1oba

Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1 complexed with choline

spinqualitylabelsall models 1oba, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1oba is a 1 chain structure with sequence from Streptococcus phage Cp1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: CHT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LYS_BPCP1 Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Strictly depends on the presence of choline-containing cell walls for activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 catalytic mechanism for the whole glycoside hydrolase family 25. Our work provides the first complete structure of a member of the large family of choline binding proteins and reveals that ChBrs are versatile elements able to tune the evolution and specificity of the pneumococcal surface proteins. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysin 3D structures Lysozyme 3D structures

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