BRENDA - Enzyme Database show

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
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.12
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)
EC Number
Commentary
Organism
2.4.1.12
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43
Rhodobacter sphaeroides
Crystallization (Commentary)
EC Number
Crystallization
Organism
2.4.1.12
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 4C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview
Rhodobacter sphaeroides
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.12
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Rhodobacter sphaeroides
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.12
Rhodobacter sphaeroides
Q3J125
-
-
Purification (Commentary)
EC Number
Commentary
Organism
2.4.1.12
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
736877
Rhodobacter sphaeroides
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
2.4.1.12
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)
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.12
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)
EC Number
Commentary
Organism
2.4.1.12
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43
Rhodobacter sphaeroides
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.4.1.12
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 4C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview
Rhodobacter sphaeroides
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.12
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Rhodobacter sphaeroides
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.12
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
736877
Rhodobacter sphaeroides
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.12
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
EC Number
General Information
Commentary
Organism
2.4.1.12
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
2.4.1.12
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)
EC Number
General Information
Commentary
Organism
2.4.1.12
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
2.4.1.12
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