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Structure paper

TitleMechanism of activation of bacterial cellulose synthase by cyclic di-GMP.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 21, Page 489-496, Year 2014
Publish dateFeb 19, 2014 (structure data deposition date)
AuthorsMorgan, J.L. / McNamara, J.T. / Zimmer, J.
External linksNat. Struct. Mol. Biol. / PubMed:24704788
MethodsX-ray diffraction
Resolution2.65 - 3.2 Å
Structure data

PDB-4p00:
Bacterial Cellulose Synthase in complex with cyclic-di-GMP and UDP
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-4p02:
Structure of Bacterial Cellulose Synthase with cyclic-di-GMP bound.
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM

ChemComp-C2E:
9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)

ChemComp-MG:
Unknown entry

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

Source
  • rhodobacter sphaeroides (bacteria)
KeywordsTRANSFERASE / membrane protein / cellulose biosynthesis / biofilm / cyclic-di-GMP / allosteric activator / biofilm formation

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