5HXD

Crystal structure of murein-tripeptide amidase MpaA from Escherichia coli O157

Summary for 5HXD

• Entry DOI: 10.2210/pdb5hxd/pdb
• Descriptor: Protein MpaA, ZINC ION, CACODYLATE ION, ... (4 entities in total)
• Functional Keywords: escherichia coli o157, mpaa, murein-tripeptide amidase, hydrolase
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 2
• Total formula weight: 52527.49

Authors

Ma, Y.,Bai, G.,Zhang, X.,Zhao, J.,Yuan, Z.,Kang, X.,Li, Z.,Mu, S.,Liu, X. (deposition date: 2016-01-30, release date: 2017-02-08, Last modification date: 2023-11-08)

Primary citation

Ma, Y.,Bai, G.,Cui, Y.,Zhao, J.,Yuan, Z.,Liu, X.
Crystal Structure of Murein-Tripeptide Amidase MpaA from Escherichia coli O157 at 2.6 angstrom Resolution
Protein Pept.Lett., 24:181-187, 2017

PubMed Abstract: 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 γ-D-Glumeso- 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 Å resolution. The asymmetric unit consists of two protein molecules and each monomer represents the common α/β fold of metallocarboxypeptidases (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.

PubMed: 27894248
DOI: 10.2174/0929866523666161128153128

Experimental method

X-RAY DIFFRACTION (2.6 Å)