Open AccessStructural insights into the enhanced carbapenemase efficiency of OXA‐655 compared to OXA‐10
Author(s) -
Leiros HannaKirsti S.,
Thomassen Ane Molden,
Samuelsen Ørjan,
Flach CarlFredrik,
Kotsakis Stathis D.,
Larsson D.G. Joakim
Publication year - 2020
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12935
Subject(s) - imipenem , chemistry , ertapenem , meropenem , carbapenem , escherichia coli , stereochemistry , residue (chemistry) , active site , hydrolysis , crystal structure , hydrolase , catalysis , enzyme , antibiotic resistance , antibiotics , biochemistry , crystallography , gene
Carbapenemases are the main cause of carbapenem resistance in Gram‐negative bacteria. OXA‐655 is a new carbapenemase variant identified from hospital wastewater. This study provides crystal structures of OXA variants bound to antibiotics to unravel the structure–function relationship and how residues impact on enzyme catalysis. The new structures illustrate how one amino acid substitution changes binding and hydrolysis of different antibiotics.