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Journal article

Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases

Abstract:

Metallo‐β‐Lactamases (MBLs) protect bacteria from almost all β‐lactam antibiotics. Verona integron‐encoded MBL (VIM) enzymes are among the most clinically important MBLs, with VIM‐1 increasing in carbapenem‐resistant Enterobacteriaceae (Escherichia coli, Klebsiella pneumoniae) that are among the hardest bacterial pathogens to treat. VIM enzymes display sequence variation at residues (224 and 228) that in related MBLs are conserved and participate in substrate binding. How they accommodate thi...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1111/febs.14695

Authors


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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0002-0137-3226
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Funding agency for:
Brem, J
Grant:
115583
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Funding agency for:
Schofield, C
Grant:
115583
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Publisher:
FEBS Press Publisher's website
Journal:
FEBS Journal Journal website
Volume:
286
Issue:
1
Pages:
169-183
Publication date:
2018-11-15
Acceptance date:
2018-11-02
DOI:
EISSN:
1742-4658
ISSN:
1742-464X
Pmid:
30430727
Source identifiers:
943655
Language:
English
Keywords:
Pubs id:
pubs:943655
UUID:
uuid:6f504f10-c741-48d8-9a3d-58acab90348f
Local pid:
pubs:943655
Deposit date:
2018-11-19

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