Structural Bioinformatics of Neisseria meningitidis LD-Carboxypeptidase: Implications for Substrate Binding and Specificity.

Autor:	Rashid, Yasmeen, Kamran Azim, M.
Předmět:	NEISSERIA meningitidis NEISSERIA GRAM-negative bacteria BACTERIA SEPSIS
Zdroj:	Protein Journal; Nov2011, Vol. 30 Issue 8, p558-565, 8p
Abstrakt:	Neisseria meningitidis, a gram negative bacterium, is the leading cause of bacterial meningitis and severe sepsis. Neisseria meningitidis genome contains 2,160 predicted coding regions including 1,000 hypothetical genes. Re-annotation of N. meningitidis hypothetical proteins identified nine putative peptidases. Among them, the NMB1620 protein was annotated as LD-carboxypeptidase involved in peptidoglycan recycling. Structural bioinformatics studies of NMB1620 protein using homology modeling and ligand docking were carried out. Structural comparison of substrate binding site of LD-carboxypeptidase was performed based on binding of tetrapeptide substrate ' l-alanyl- d-glutamyl-meso-diaminopimelyl- d-alanine'. Inspection of different subsite-forming residues showed changeability in the S1 subsite across different bacterial species. This variability was predicted to provide a structural basis to S1-subsite for accommodating different amino acid residues at P1 position of the tetrapeptide substrate ' l-alanyl- d-glutamyl-meso-diaminopimelyl- d-alanine'. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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