1oba

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|PDB= 1oba |SIZE=350|CAPTION= <scene name='initialview01'>1oba</scene>, resolution 2.45&Aring;
|PDB= 1oba |SIZE=350|CAPTION= <scene name='initialview01'>1oba</scene>, resolution 2.45&Aring;
|SITE= <scene name='pdbsite=CH1:Cht+Binding+Site+For+Chain+A'>CH1</scene>
|SITE= <scene name='pdbsite=CH1:Cht+Binding+Site+For+Chain+A'>CH1</scene>
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|LIGAND= <scene name='pdbligand=CHT:CHOLINE ION'>CHT</scene>
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|LIGAND= <scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oba OCA], [http://www.ebi.ac.uk/pdbsum/1oba PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oba RCSB]</span>
}}
}}
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[[Category: Menendez, M.]]
[[Category: Menendez, M.]]
[[Category: Monterroso, B.]]
[[Category: Monterroso, B.]]
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[[Category: CHT]]
 
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[[Category: bacterilytic enzyme]]
 
[[Category: choline]]
[[Category: choline]]
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[[Category: hydrolase glycosidase]]
 
[[Category: lysozyme]]
[[Category: lysozyme]]
[[Category: multimodular]]
[[Category: multimodular]]
[[Category: murein hydrolase]]
[[Category: murein hydrolase]]
[[Category: phage cp-1 lysin]]
[[Category: phage cp-1 lysin]]
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[[Category: pneumococcal cell wall degradation]]
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[[Category: pneumococcal cell wall degradation,hydrolase glycosidase,bacterilytic enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:40 2008''

Revision as of 19:42, 30 March 2008


PDB ID 1oba

Drag the structure with the mouse to rotate
, resolution 2.45Å
Sites:
Ligands:
Activity: Lysozyme, with EC number 3.2.1.17
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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