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TitleThe importance of the trans-enamine intermediate as a beta-lactamase inhibition strategy probed in inhibitor-resistant SHV beta-lactamase variants.
Journal, issue, pagesChemmedchem, Vol. 7, Page 1002-1008, Year 2012
Publish dateDec 15, 2011 (structure data deposition date)
AuthorsKe, W. / Rodkey, E.A. / Sampson, J.M. / Skalweit, M.J. / Sheri, A. / Pagadala, S.R. / Nottingham, M.D. / Buynak, J.D. / Bonomo, R.A. / van den Akker, F.
External linksChemmedchem / PubMed:22438274
MethodsX-ray diffraction
Resolution1.3 - 1.45 Å
Structure data

PDB-3v50:
Complex of SHV S130G mutant beta-lactamase complexed to SA2-13
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-3v5m:
Crystal structure of M69V mutant of SHV beta-lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-SA2:
(3R)-4-[(4-CARBOXYBUTANOYL)OXY]-N-[(1E)-3-OXOPROP-1-EN-1-YL]-3-SULFINO-D-VALINE

ChemComp-MA4:
CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE

ChemComp-HOH:
WATER

Source
  • klebsiella pneumoniae (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / class A beta-lactamase fold / hydrolyze b-lactam antibiotics / HYDROLASE-HYDROLASE INHIBITOR complex / HYDROLASE

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