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Structure paper

TitleQuantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 109, Page E299-E308, Year 2013
Publish dateSep 20, 2010 (structure data deposition date)
AuthorsSigala, P.A. / Fafarman, A.T. / Schwans, J.P. / Fried, S.D. / Fenn, T.D. / Caaveiro, J.M. / Pybus, B. / Ringe, D. / Petsko, G.A. / Boxer, S.G. / Herschlag, D.
External linksProc. Natl. Acad. Sci. USA / PubMed:23798390
MethodsX-ray diffraction
Resolution1.3 - 1.71 Å
Structure data

PDB-3ows:
Crystal Structure of Ketosteroid Isomerase D40N/C69S/C81S/C97S/M116C-CN from P. putida with Bound Equilenin
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-3vgn:
Crystal Structure of Ketosteroid Isomerase D40N from Pseudomonas putida (pKSI) with bound 3-fluoro-4-nitrophenol
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-EQU:
EQUILENIN

ChemComp-HOH:
WATER

ChemComp-FNN:
3-fluoro-4-nitrophenol

Source
  • pseudomonas putida (bacteria)
KeywordsISOMERASE / Steroid / Cyanylation / hydrogen bond / KSI / enzyme catalysis / transition state / oxyanion hole

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