1oba

From Proteopedia

Revision as of 13:44, 30 October 2007

MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1 COMPLEXED WITH CHOLINE

Overview

Pneumococcal bacteriophage-encoded lysins are modular choline binding, proteins that have been shown to act as enzymatic antimicrobial agents, (enzybiotics) against streptococcal infections. Here we present the, crystal structures of the free and choline bound states of the Cpl-1, lysin, encoded by the pneumococcal phage Cp-1. While the catalytic module, displays an irregular (beta/alpha)(5)beta(3) barrel, the cell, wall-anchoring module is formed by six similar choline binding repeats, (ChBrs), arranged into two different structural regions: a left-handed, superhelical domain configuring two choline binding sites, and a beta, sheet domain that contributes in bringing together the whole structure., Crystallographic and site-directed mutagenesis studies allow us to propose, a general ... [(full description)]

About this Structure

1OBA is a [Single protein] structure of sequence from [Bacteriophage cp-1] with CHT as [ligand]. Active as [Lysozyme], with EC number [3.2.1.17]. Structure known Active Site: CH1. Full crystallographic information is available from [OCA].

Reference

Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1., Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M, Structure. 2003 Oct;11(10):1239-49. PMID:14527392

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