BRENDA - Enzyme Database show
show all sequences of 2.4.1.12

Crystallographic snapshot of cellulose synthesis and membrane translocation

Morgan, J.L.W.; Strumillo, J.; Zimmer, J.; Nature 493, 181-186 (2013)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
cyclic-di-GMP
BcsA contains a PilZ domain within its C-terminal, intracellular domain and its activity is strongly stimulated by the bacterial secondary messenger cyclic-di-GMP
Rhodobacter sphaeroides
Cloned(Commentary)
Commentary
Organism
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43
Rhodobacter sphaeroides
Crystallization (Commentary)
Crystallization
Organism
purified recombinant native and selenomethionine -labeled complex of BcsA and BcsB containing a translocating polysaccharide, from 30% PEG 200, 0.1 M MES, pH 6.5, and 50 mM NaCl at 4°C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview
Rhodobacter sphaeroides
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
inner membrane
cellulose synthases are membrane-embedded glycosyltransferases. BcsB is a periplasmic protein that is anchored to the inner membrane via a single, C-terminal transmembrane helix. BcsA and BcsB are fused
Rhodobacter sphaeroides
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Rhodobacter sphaeroides
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
Q3J125
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged native and selenomethionine -labeled subunits BcsA and B from Escherichia coli strain C43 by nickel affinity chromatography and gel filtration
Rhodobacter sphaeroides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
736877
Rhodobacter sphaeroides
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
BcsA and BcsB form a 1:1 stoichiometric complex spanning approximately 150 A perpendicular and 55 A parallel to the membrane. The complex is divided into a cuboid-shaped membrane-spanning region sandwiched between large cytoplasmic and periplasmic domains. BcsA contains four N-terminal and four C-terminal transmembrane-helices separated by a large intracellular loop (4/5-loop) that forms a GT-domain (aa 128 to 368). transmembrane domains 3-8 form a narrow channel for the translocating polysaccharide and BcsA's intracellular C-terminus (aa 575 to 759) contains a 6-stranded beta-barrel and a highly curved alpha-helical region that attaches the beta-barrel to the GT-domain. BcsB is a dome-shaped, beta-strand rich, periplasmic protein. Its N-terminal region forms the tip of the dome, whereas the C-terminal transmembrane-anchor interacts with BcsA. Two amphipathic helices further stabilize its interaction with BcsA and the periplasmic water-membrane interface. Domain structures. Modeling, overview
Rhodobacter sphaeroides
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
cyclic-di-GMP
BcsA contains a PilZ domain within its C-terminal, intracellular domain and its activity is strongly stimulated by the bacterial secondary messenger cyclic-di-GMP
Rhodobacter sphaeroides
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43
Rhodobacter sphaeroides
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant native and selenomethionine -labeled complex of BcsA and BcsB containing a translocating polysaccharide, from 30% PEG 200, 0.1 M MES, pH 6.5, and 50 mM NaCl at 4°C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview
Rhodobacter sphaeroides
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
inner membrane
cellulose synthases are membrane-embedded glycosyltransferases. BcsB is a periplasmic protein that is anchored to the inner membrane via a single, C-terminal transmembrane helix. BcsA and BcsB are fused
Rhodobacter sphaeroides
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Rhodobacter sphaeroides
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged native and selenomethionine -labeled subunits BcsA and B from Escherichia coli strain C43 by nickel affinity chromatography and gel filtration
Rhodobacter sphaeroides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
736877
Rhodobacter sphaeroides
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
BcsA and BcsB form a 1:1 stoichiometric complex spanning approximately 150 A perpendicular and 55 A parallel to the membrane. The complex is divided into a cuboid-shaped membrane-spanning region sandwiched between large cytoplasmic and periplasmic domains. BcsA contains four N-terminal and four C-terminal transmembrane-helices separated by a large intracellular loop (4/5-loop) that forms a GT-domain (aa 128 to 368). transmembrane domains 3-8 form a narrow channel for the translocating polysaccharide and BcsA's intracellular C-terminus (aa 575 to 759) contains a 6-stranded beta-barrel and a highly curved alpha-helical region that attaches the beta-barrel to the GT-domain. BcsB is a dome-shaped, beta-strand rich, periplasmic protein. Its N-terminal region forms the tip of the dome, whereas the C-terminal transmembrane-anchor interacts with BcsA. Two amphipathic helices further stabilize its interaction with BcsA and the periplasmic water-membrane interface. Domain structures. Modeling, overview
Rhodobacter sphaeroides
General Information
General Information
Commentary
Organism
additional information
structure of the BcsA-B translocation intermediate revealing the architecture of the cellulose synthase. Subunit BcsA forms a cellulose-conducting channel, modeling for the coupling of cellulose synthesis and translocation in which the nascent polysaccharide is extended by one glucose molecule at a time, overview
Rhodobacter sphaeroides
physiological function
cellulose synthases (CESAs) are membrane-embedded glycosyltransferases, which utilize UDP-activated glucose (UDP-Glc) to processively elongate the nascent polysaccharide in a reaction that inverts the configuration at the anomeric carbon of the newly added sugar from alpha to beta. Cellulose synthesis and transport across the inner bacterial membrane is mediated by a complex of the multi-spanning catalytic BcsA subunit and the membrane-anchored, periplasmic BcsB protein. Structure-function analysis and modeling, overview
Rhodobacter sphaeroides
General Information (protein specific)
General Information
Commentary
Organism
additional information
structure of the BcsA-B translocation intermediate revealing the architecture of the cellulose synthase. Subunit BcsA forms a cellulose-conducting channel, modeling for the coupling of cellulose synthesis and translocation in which the nascent polysaccharide is extended by one glucose molecule at a time, overview
Rhodobacter sphaeroides
physiological function
cellulose synthases (CESAs) are membrane-embedded glycosyltransferases, which utilize UDP-activated glucose (UDP-Glc) to processively elongate the nascent polysaccharide in a reaction that inverts the configuration at the anomeric carbon of the newly added sugar from alpha to beta. Cellulose synthesis and transport across the inner bacterial membrane is mediated by a complex of the multi-spanning catalytic BcsA subunit and the membrane-anchored, periplasmic BcsB protein. Structure-function analysis and modeling, overview
Rhodobacter sphaeroides
Other publictions for EC 2.4.1.12
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736991
Olek
The structure of the catalytic ...
Oryza sativa
Plant Cell
26
2996-3009
2014
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736877
Morgan
Crystallographic snapshot of c ...
Rhodobacter sphaeroides
Nature
493
181-186
2013
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737161
Omadjela
BcsA and BcsB form the catalyt ...
Rhodobacter sphaeroides
Proc. Natl. Acad. Sci. USA
110
17856-17861
2013
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2
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718750
Fugelstad
Functional characterization of ...
Saprolegnia monoica
Biochem. Biophys. Res. Commun.
417
1248-1253
2012
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2
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702850
Lau
-
Molecular cloning of cellulose ...
Shorea parvifolia
Biotechnology
8
416-424
2009
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1
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702925
Yin
The cellulose synthase superfa ...
Arabidopsis thaliana, Oryza sativa, Phaeodactylum tricornutum, Populus trichocarpa, Selaginella moellendorffii, Sorghum bicolor, Vitis vinifera
BMC Plant Biol.
9
99-112
2009
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7
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703730
Timmers
Interactions between membrane- ...
Arabidopsis thaliana
FEBS Lett.
583
978-982
2009
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1
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8
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1
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5
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3
6
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1
3
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703825
Fugelstad
Identification of the cellulos ...
Saprolegnia monoica
Fungal Genet. Biol.
46
759-767
2009
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1
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2
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2
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1
1
2
2
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704608
Atanassov
Elucidating the mechanisms of ...
Arabidopsis thaliana
J. Biol. Chem.
284
3833-3841
2009
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1
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5
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1
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1
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705822
Sandhu
Plant cell wall matrix polysac ...
Arabidopsis thaliana, Hordeum vulgare, Oryza sativa
Mol. Plant
2
840-850
2009
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2
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3
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705949
Daras
The thanatos mutation in Arabi ...
Arabidopsis thaliana
New Phytol.
184
114-126
2009
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706179
Wightman
A cellulose synthase-containin ...
Arabidopsis thaliana
Plant Cell Physiol.
50
584-594
2009
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2
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706267
Obembe
Differential expression of cel ...
Solanum tuberosum
Plant Physiol. Biochem.
47
1116-1118
2009
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1
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706876
Kumar
An update on the nomenclature ...
Arabidopsis thaliana, Populus alba, Populus balsamifera, Populus deltoides, Populus euphratica, Populus nigra, Populus simonii, Populus tremula, Populus tremula x Populus alba, Populus tremula x Populus tremuloides, Populus tremuloides, Populus trichocarpa, Populus trichocarpa x Populus deltoides, Populus x canadensis, Populus x tomentiglandulosa
Trends Plant Sci.
14
248-254
2009
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15
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18
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15
15
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685834
Singh
Insight into the early steps o ...
Arabidopsis thaliana
BMC Plant Biol.
8
57
2008
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689478
Grenville-Briggs
Cellulose synthesis in Phytoph ...
Phytophthora infestans
Plant Cell
20
720-738
2008
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689619
Paredez
Genetic evidence that cellulos ...
Arabidopsis thaliana
Plant Physiol.
147
1723-1734
2008
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704868
Lu
Differential expression of thr ...
Eucalyptus grandis
J. Exp. Bot.
59
681-695
2008
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1
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689555
Taylor
Identification of cellulose sy ...
Arabidopsis thaliana
Plant Mol. Biol.
64
161-171
2007
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676809
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661462
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Cellulose synthesis in the Ara ...
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637180
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Modifications of cellulose syn ...
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637181
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Cellulose in cyanobacteria. Or ...
Anabaena sp., Crinalium epipsammum, Desmonostoc muscorum, Gloeocapsa sp., Nostoc punctiforme, Oscillatoria princeps, Oscillatoria sp., Phormidium autumnale, Scytonema hofmannii
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637176
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PROCUSTE1 encodes a cellulose ...
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Thermal stability of the cellu ...
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637179
Saxena
-
Identification of cellulose sy ...
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Cellulose
4
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1997
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637174
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beta-Glucan synthesis in cotto ...
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Cyclic diguanylic acid stimula ...
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Congo red inhibits in vitro be ...
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Haass
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Orientation of cell wall beta- ...
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Solubilization of the UDP-gluc ...
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Achievement of high rates of i ...
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Larsen
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beta-(1->4)-D-glucan synthesis ...
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The synthesis of cellulose in ...
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