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Structure paper

TitleThe Reaction Mechanism of Metallo-beta-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop.
Journal, issue, pagesAntimicrob. Agents Chemother., Vol. 63, Year 2019
Publish dateJan 18, 2018 (structure data deposition date)
AuthorsPalacios, A.R. / Mojica, M.F. / Giannini, E. / Taracila, M.A. / Bethel, C.R. / Alzari, P.M. / Otero, L.H. / Klinke, S. / Llarrull, L.I. / Bonomo, R.A. / Vila, A.J.
External linksAntimicrob. Agents Chemother. / PubMed:30348667
MethodsX-ray diffraction
Resolution1.65 - 1.79 Å
Structure data

PDB-6c6i:
Crystal structure of a chimeric NDM-1 metallo-beta-lactamase harboring the IMP-1 L3 loop
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6cac:
Crystal structure of NDM-1 metallo-beta-lactamase harboring an insertion of a Pro residue in L3 loop
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CD:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-CO:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-SO4:
SULFATE ION

Source
  • klebsiella pneumoniae (bacteria)
KeywordsHYDROLASE / Chimeric protein / NDM-1 / Zn-contaning protein / Zn-containing protein

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