Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein
Structure and Function of the First Full-Length Murein Peptide Ligase (Mpl) Cell Wall Recycling Protein Debanu Das1,2, Mireille Herve´ 3,4, Julie Feuerhelm1,5, Carol L. Farr1,6, Hsiu-Ju Chiu1,2, Marc-Andre´ Elsliger1,6, Mark W. Knuth1,5, Heath E. Klock1,5, Mitchell D. Miller1,2, Adam Godzik1,7,8, Scott A. Lesley1,5,6, Ashley M. Deacon1,2, Dominique Mengin-Lecreulx3,4*, Ian A. Wilson1,6* 1 Joint Center for Structural Genomics ( http://www.jcsg.org), 2 Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California, United States of America, 3 Universite´ Paris-Sud, Laboratoire des Enveloppes Bacte´riennes et Antibiotiques, Orsay, France, 4 Centre National de la Recherche Scientifique, Institut de Biochimie et Biophysique Mole´culaire et Cellulaire, Orsay, France, 5 Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California, United States of America, 6 Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, United States of America, 7 Center for Research in Biological Systems, University of California San Diego, La Jolla, California, United States of America, 8 Program on Bioinformatics and Systems Biology, Sanford- Burnham Medical Research Institute, La Jolla, California, United States of America Abstract 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).
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