Journal article icon

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...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

Actions


Access Document


Files:
Publisher copy:
10.1111/febs.14695

Authors


Salimraj, R More by this author
Hinchliffe, P More by this author
Kosmopoulou, M More by this author
Tyrrell, JM More by this author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
ORCID:
0000-0002-0137-3226
Expand authors...
More from this funder
Funding agency for:
Schofield, CJ
Expand funders...
Publisher:
FEBS Press Publisher's website
Journal:
The 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
Pubs id:
pubs:943655
URN:
uri:6f504f10-c741-48d8-9a3d-58acab90348f
UUID:
uuid:6f504f10-c741-48d8-9a3d-58acab90348f
Local pid:
pubs:943655

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP