1oba
From Proteopedia
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| - | [[Image:1oba.gif|left|200px]]<br /><applet load="1oba" size=" | + | [[Image:1oba.gif|left|200px]]<br /><applet load="1oba" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oba, resolution 2.45Å" /> | caption="1oba, resolution 2.45Å" /> | ||
'''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1 COMPLEXED WITH CHOLINE'''<br /> | '''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1 COMPLEXED WITH CHOLINE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OBA 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] with CHT as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=CH1:Cht Binding Site For Chain A'>CH1</scene>. Full crystallographic information is available from [http:// | + | 1OBA 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] with <scene name='pdbligand=CHT:'>CHT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=CH1:Cht+Binding+Site+For+Chain+A'>CH1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBA OCA]. |
==Reference== | ==Reference== | ||
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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 Sun Feb 3 09:55:48 2008'' |
Revision as of 07:55, 3 February 2008
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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 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
1OBA is a Single protein structure of sequence from Bacteriophage cp-1 with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Site: . 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 Sun Feb 3 09:55:48 2008
Categories: Bacteriophage cp-1 | Lysozyme | Single protein | Albert, A. | Garcia, J.L. | Garcia, P. | Hermoso, J.A. | Martinez-Ripoll, M. | Menendez, M. | Monterroso, B. | CHT | Bacterilytic enzyme | Choline | Hydrolase glycosidase | Multimodular | Murein hydrolase | Phage cp-1 lysin | Pneumococcal cell wall degradation
