Putting a stop to L,D-transpeptidases

Soumya De; Lawrence P McIntosh

doi:10.1016/j.str.2012.04.005

Putting a stop to L,D-transpeptidases

Structure. 2012 May 9;20(5):753-4. doi: 10.1016/j.str.2012.04.005.

Authors

Soumya De¹, Lawrence P McIntosh

Affiliation

¹ Department of Biochemistry and Molecular Biology, Department of Chemistry, and Michael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z3, Canada. somde@chem.ubc.ca

PMID: 22579243
DOI: 10.1016/j.str.2012.04.005

Abstract

In this issue of Structure, Lecoq et al. investigated the structural and dynamic basis for the unexpected inhibition of peptidoglycan-crosslinking l,d-transpeptidases by carbapenem antibiotics. In addition to defining a neutral thiol-imidazole catalytic triad, their studies revealed extensive induced motions upon formation of a long-live covalent drug-enzyme complex.

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