2j8f: Difference between revisions

Pneumococcal bacteriophage-encoded lysins are modular proteins that have, been shown to act as enzymatic antimicrobial agents (enzybiotics) in, treatment of streptococcal infections. The first X-ray crystal structures, of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1, in complex, with three bacterial cell wall peptidoglycan (PG) analogues are reported, herein. The Cpl-1 structure is folded in two well-defined modules, one, responsible for anchoring to the pneumococcal cell wall and the other, a, catalytic module, that hydrolyzes the PG. Conformational rearrangement of, Tyr127 is a critical event in molecular recognition of a stretch of five, saccharide rings of the polymeric peptidoglycan (cell wall). The PG is, bound at a stretch of the surface that is defined as the, peptidoglycan-binding sites 1 and 2 at the juncture of which catalysis, takes place. The peptidoglycan-binding site 1 binds to a stretch of three, saccharides of the peptidoglycan in a conformation essentially identical, to that of the peptidoglycan in solution. In contrasts binding of two, peptidoglycan saccharides at the peptidoglycan-binding site 2 introduces a, kink into the solution structure of the peptidoglycan, en route to, catalytic turnover. These findings provide the first structural evidence, on recognition of the peptidoglycan and shed light on the discrete events, of cell wall degradation by Cpl-1.

2J8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_cp-1 Bacteriophage cp-1] with NAG, ALA, AMV, DGL and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J8F OCA].  

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