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| {{STRUCTURE_1h09| PDB=1h09 | SCENE= }} | | {{STRUCTURE_1h09| PDB=1h09 | SCENE= }} |
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| '''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1'''
| | ===MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14527392}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14527392 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14527392}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Murein hydrolase]] | | [[Category: Murein hydrolase]] |
| [[Category: Pneumococcal cell wall degradation]] | | [[Category: Pneumococcal cell wall degradation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:15:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:24:26 2008'' |
