5hxd

Publication Abstract from PubMed

Peptidoglycan (PG) is an essential component of the cell wall, and undergoes reconstruction by various PG hydrolases during cell growth, development and division. The murein- tripeptide (Mtp) amidase MpaA belongs to PG hydrolase family and is responsible for cleaving the gamma-D-Glu-meso-Dap amide bond in the Mtp released during PG turnover. The current paper reports the crystal structure of MpaA from Escherichia coli (E. coli) O157 at 2.6 A resolution. The asymmetric unit consists of two protein molecules and each monomer represents the common alpha/beta fold of metallo-carboxypeptidases (MCP). The Tyr133-Asp143 loop appears to mediate the entrance and binding of the substrate into the active groove. A structural comparison of MpaA with its homologue from Vibrio harveyi showed that MpaA has narrower active pocket entrance with a smaller surface opening, which is determined by the Val204-Thr211 loop. The reported structure provides a starting point for the molecular mechanism of MpaA in a significant human pathogen.

Crystal Structure of Murein-Tripeptide Amidase MpaA from Escherichia coli O157 at 2.6 A Resolution.,Ma Y, Bai G, Cui Y, Zhao J, Yuan Z, Liu X Protein Pept Lett. 2016 Nov 28. PMID:27894248^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.