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Structure paper

TitleStructural insights into the mechanism of c-di-GMP-bound YcgR regulating flagellar motility inEscherichia coli.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 808-821, Year 2020
Publish dateAug 11, 2017 (structure data deposition date)
AuthorsHou, Y.J. / Yang, W.S. / Hong, Y. / Zhang, Y. / Wang, D.C. / Li, D.F.
External linksJ. Biol. Chem. / PubMed:31836667
MethodsX-ray diffraction
Resolution1.774 - 2.3 Å
Structure data

PDB-5y6f:
Crystal structure of YcgR in complex with c-di-GMP from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5y6g:
PilZ domain with c-di-GMP of YcgR from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5y6h:
Crystal structure of YcgR-N domain of YcgR from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 1.774 Å

Chemicals

ChemComp-SO4:
SULFATE ION

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-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli k-12 (bacteria)
KeywordsPROTEIN BINDING / C-di-GMP binding / Flagellar brake protein / Motor protein binding / PilZ domain / UNKNOWN FUNCTION / YcgR-N domain / YcgR

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