Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase

Kim, Youngchang; Tesar, Christine; Mire, Joseph; Jedrzejczak, Robert; Binkowski, Andrew; Babnigg, Gyorgy; Sacchettini, James; Joachimiak, Andrzej

doi:10.1371/journal.pone.0024621

Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase

Journal Article · Thu Sep 08 00:00:00 EDT 2011 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0024621· OSTI ID:1627473

Kim, Youngchang ^[1]; Tesar, Christine ^[2]; Mire, Joseph ^[3]; Jedrzejczak, Robert ^[4]; Binkowski, Andrew ^[4]; Babnigg, Gyorgy ^[4]; Sacchettini, James ^[3]; Joachimiak, Andrzej ^[5]

Argonne National Lab. (ANL), Argonne, IL (United States). Biosciences. Midwest Center for Structural Genomics and Structural Biology; DOE/OSTI
Argonne National Lab. (ANL), Argonne, IL (United States)
Texas A & M Univ., College Station, TX (United States). Dept. of Biochemistry and Biophysics
Argonne National Lab. (ANL), Argonne, IL (United States). Biosciences. Midwest Center for Structural Genomics and Structural Biology
Argonne National Lab. (ANL), Argonne, IL (United States). Biosciences. Midwest Center for Structural Genomics and Structural Biology; Univ. of Chicago, IL (United States). Dept. of Molecular Genetics and Cell Biology

The New Delhi Metallo-b-lactamase (NDM-1) gene makes multiple pathogenic microorganisms resistant to all known blactam antibiotics. The rapid emergence of NDM-1 has been linked to mobile plasmids that move between different strains resulting in world-wide dissemination. Biochemical studies revealed that NDM-1 is capable of efficiently hydrolyzing a wide range of b-lactams, including many carbapenems considered as ‘‘last resort’’ antibiotics. The crystal structures of metal-free apo- and monozinc forms of NDM-1 presented here revealed an enlarged and flexible active site of class B1 metallo-blactamase. This site is capable of accommodating many b-lactam substrates by having many of the catalytic residues on flexible loops, which explains the observed extended spectrum activity of this zinc dependent b-lactamase. Indeed, five loops contribute ‘‘keg’’ residues in the active site including side chains involved in metal binding. Loop 1 in particular, shows conformational flexibility, apparently related to the acceptance and positioning of substrates for cleavage by a zinc-activated water molecule.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1627473

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 9 Vol. 6; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Extended-spectrum β -Lactamases: Implications for the Clinical Laboratory and Therapy Harada, Sohei; Ishii, Yoshikazu; Yamaguchi, Keizo Annals of Laboratory Medicine, Vol. 28, Issue 6 https://doi.org/10.3343/kjlm.2008.28.6.401	journal	December 2008
Multidrug-resistant Enterobacteriaceae including metallo-β-lactamase producers are predominant pathogens of healthcare-associated infections in an Indian teaching hospital Sarma, Jb; Bhattacharya, Pk; Kalita, D. Indian Journal of Medical Microbiology, Vol. 29, Issue 1 https://doi.org/10.4103/0255-0857.76519	journal	January 2011

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Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida Tu, Xiongying; Latham, John A.; Klema, Valerie J. JBIC Journal of Biological Inorganic Chemistry, Vol. 22, Issue 7 https://doi.org/10.1007/s00775-017-1486-8	journal	August 2017
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Refined Models of New Delhi metallo-beta-lactamase-1 with Inhibitors: An QM/MM Modeling Study Wang, Yeng-Tseng; Cheng, Tian-Lu Taylor & Francis https://doi.org/10.6084/m9.figshare.1581516.v1	text	January 2015
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