Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein

Das, Debanu; Hervé, Mireille; Feuerhelm, Julie; Farr, Carol L.; Chiu, Hsiu-Ju; Elsliger, Marc-André; Knuth, Mark W.; Klock, Heath E.; Miller, Mitchell D.; Godzik, Adam; Lesley, Scott A.; Deacon, Ashley M.; Mengin-Lecreulx, Dominique; Wilson, Ian A.

doi:10.1371/journal.pone.0017624

Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein

Journal Article · Fri Mar 18 00:00:00 EDT 2011 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0017624· OSTI ID:1627447

Das, Debanu ^[1]; Hervé, Mireille ^[2]; Feuerhelm, Julie ^[3]; Farr, Carol L. ^[4]; Chiu, Hsiu-Ju ^[5]; Elsliger, Marc-André ^[4]; Knuth, Mark W. ^[3]; Klock, Heath E. ^[3]; Miller, Mitchell D. ^[5]; Godzik, Adam ^[6]; Lesley, Scott A. ^[7]; Deacon, Ashley M. ^[5]; Mengin-Lecreulx, Dominique ^[2]; Wilson, Ian A. ^[4]

Joint Center for Structural Genomics (http://www.jcsg.org) (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL); DOE/OSTI
Universite Paris-Sud, Orsay (France). Laboratoire des Enveloppes Bacteriennes et Antibiotiques; Centre National de la Recherche Scientifique (CNRS), Orsay (France). Institut de Biochimie et Biophysique Moleculaire et Cellulaire
Joint Center for Structural Genomics (http://www.jcsg.org) (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
Joint Center for Structural Genomics (http://www.jcsg.org) (United States); The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
Joint Center for Structural Genomics (http://www.jcsg.org) (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Joint Center for Structural Genomics (http://www.jcsg.org) (United States); Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems; Sanford-Burnham Medical Research Institute, La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
Joint Center for Structural Genomics (http://www.jcsg.org) (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.; The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology

Bacterial cell walls contain peptidoglycan, an essential polymer made by enzymes in the Mur pathway. These proteins are specific to bacteria, which make them targets for drug discovery. MurC, MurD, MurE and MurF catalyze the synthesis of the peptidoglycan precursor UDP-N-acetylmuramoyl-L-alanyl-c-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine by the sequential addition of amino acids onto UDP-N-acetylmuramic acid (UDP-MurNAc). MurC-F enzymes have been extensively studied by biochemistry and X-ray crystallography. In Gram-negative bacteria, ~30–60% of the bacterial cell wall is recycled during each generation. Part of this recycling process involves the murein peptide ligase (Mpl), which attaches the breakdown product, the tripeptide L-alanyl-c-D-glutamyl-meso-diaminopimelate, to UDP-MurNAc. We present the crystal structure at 1.65 Å resolution of a full-length Mpl from the permafrost bacterium Psychrobacter arcticus 273-4 (PaMpl). Although the Mpl structure has similarities to Mur enzymes, it has unique sequence and structure features that are likely related to its role in cell wall recycling, a function that differentiates it from the MurC-F enzymes. We have analyzed the sequence-structure relationships that are unique to Mpl proteins and compared them to MurC-F ligases. We have also characterized the biochemical properties of this enzyme (optimal temperature, pH and magnesium binding profiles and kinetic parameters). Although the structure does not contain any bound substrates, we have identified ~30 residues that are likely to be important for recognition of the tripeptide and UDP-MurNAc substrates, as well as features that are unique to Psychrobacter Mpl proteins. These results provide the basis for future mutational studies for more extensive function characterization of the Mpl sequence-structure relationships.

View Accepted Manuscript (DOE)

Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); USDOE Office of Science (SC), Basic Energy Sciences (BES); National Center for Research Resources (NCRR)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1627447

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 3 Vol. 6; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Crystal structure
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Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein

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