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2ixv
From Proteopedia
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CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A PEPTIDOGLYCAN ANALOGUE (E94Q MUTANT)
Overview
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, ... [(full description)]
About this Structure
2IXV is a [Single protein] structure of sequence from [Streptococcus phage cp-1] with NAG, MU2 and FMT as [ligands]. Active as [Lysozyme], with EC number [3.2.1.17]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1., Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA, J Biol Chem. 2007 Jun 19;. PMID:17581815
Page seeded by OCA on Tue Oct 30 17:19:07 2007
