1h09
From Proteopedia
(New page: 200px<br /><applet load="1h09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h09, resolution 2.1Å" /> '''MULTIMODULAR PNEUMOCO...) |
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| - | [[Image:1h09.gif|left|200px]]<br /><applet load="1h09" size=" | + | [[Image:1h09.gif|left|200px]]<br /><applet load="1h09" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h09, resolution 2.1Å" /> | caption="1h09, resolution 2.1Å" /> | ||
'''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1'''<br /> | '''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pneumococcal bacteriophage-encoded lysins are modular choline binding | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1H09 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]. 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] Full crystallographic information is available from [http:// | + | 1H09 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]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H09 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Albert, A.]] | [[Category: Albert, A.]] | ||
| - | [[Category: Garcia, J | + | [[Category: Garcia, J L.]] |
[[Category: Garcia, P.]] | [[Category: Garcia, P.]] | ||
| - | [[Category: Hermoso, J | + | [[Category: Hermoso, J A.]] |
[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
[[Category: Menendez, M.]] | [[Category: Menendez, M.]] | ||
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[[Category: pneumococcal cell wall degradation]] | [[Category: pneumococcal cell wall degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:02 2008'' |
Revision as of 10:56, 21 February 2008
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MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1
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 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.
About this Structure
1H09 is a Single protein structure of sequence from Bacteriophage cp-1. Active as Lysozyme, with EC number 3.2.1.17 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
Page seeded by OCA on Thu Feb 21 12:56:02 2008
