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Structure paper

TitleStructural Basis for the Inhibition of Host Protein Ubiquitination by Shigella Effector Kinase OspG.
Journal, issue, pagesStructure, Vol. 22, Page 878-888, Year 2014
Publish dateApr 16, 2014 (structure data deposition date)
AuthorsGrishin, A.M. / Condos, T.E. / Barber, K.R. / Campbell-Valois, F.X. / Parsot, C. / Shaw, G.S. / Cygler, M.
External linksStructure / PubMed:24856362
MethodsX-ray diffraction
Resolution1.869 - 1.999 Å
Structure data

PDB-4q5e:
Shigella Effector Kinase OspG bound to E2-Ub UbcH7-Ub Conjugate
Method: X-RAY DIFFRACTION / Resolution: 1.869 Å

PDB-4q5h:
Shigella Effector Kinase OspG bound to AMPPNP and E2-Ub UbcH7-Ub Conjugate
Method: X-RAY DIFFRACTION / Resolution: 1.999 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • shigella sonnei ss046 (bacteria)
  • saccharomyces cerevisiae (brewer's yeast)
  • homo sapiens (human)
  • shigella sonnei (bacteria)
KeywordsUNKNOWN FUNCTION / PROTEIN BINDING / protein-protein complex / Structural Genomics / Montreal-Kingston Bacterial Structural Genomics Initiative / BSGI / kinase fold / inhibition of NF-kB pathway

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