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Literature summary extracted from

  • Morgan, J.L.W.; Strumillo, J.; Zimmer, J.
    Crystallographic snapshot of cellulose synthesis and membrane translocation (2013), Nature, 493, 181-186.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment 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 Cereibacter sphaeroides

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.12 recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43 Cereibacter sphaeroides

Crystallization (Commentary)

EC Number Crystallization (Comment) 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 4°C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview Cereibacter sphaeroides

Localization

EC Number Localization Comment 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 Cereibacter sphaeroides
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-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.12 UDP-glucose + [(1->4)-beta-D-glucosyl]n Cereibacter sphaeroides
-
 UDP + [(1->4)-beta-D-glucosyl]n+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.12 Cereibacter sphaeroides Q3J125
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-

Purification (Commentary)

EC Number Purification (Comment) 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 Cereibacter sphaeroides

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.12 UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
 Cereibacter sphaeroides UDP + [(1->4)-beta-D-glucosyl]n+1
-
 ?

Subunits

EC Number Subunits Comment 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 Cereibacter sphaeroides

Synonyms

EC Number Synonyms Comment Organism
2.4.1.12 BcsA-B
-
 Cereibacter sphaeroides
2.4.1.12 inner membrane-associated bacterial cellulose synthase
-
 Cereibacter sphaeroides

General Information

EC Number General Information Comment 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 Cereibacter 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 Cereibacter sphaeroides