1h09

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[[Image:1h09.gif|left|200px]]
 
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{{Structure
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==Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1==
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|PDB= 1h09 |SIZE=350|CAPTION= <scene name='initialview01'>1h09</scene>, resolution 2.1&Aring;
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<StructureSection load='1h09' size='340' side='right'caption='[[1h09]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1h09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_phage_Cp1 Streptococcus phage Cp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H09 FirstGlance]. <br>
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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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h09 OCA], [https://pdbe.org/1h09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h09 RCSB], [https://www.ebi.ac.uk/pdbsum/1h09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h09 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h09 OCA], [http://www.ebi.ac.uk/pdbsum/1h09 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h09 RCSB]</span>
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[https://www.uniprot.org/uniprot/LYS_BPCP1 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.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/1h09_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h09 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:14527392</ref>
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1H09 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_cp-1 Bacteriophage cp-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H09 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14527392 14527392]
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</div>
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[[Category: Bacteriophage cp-1]]
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<div class="pdbe-citations 1h09" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Albert, A.]]
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[[Category: Garcia, J L.]]
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[[Category: Garcia, P.]]
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[[Category: Hermoso, J A.]]
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[[Category: Martinez-Ripoll, M.]]
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[[Category: Menendez, M.]]
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[[Category: Monterroso, B.]]
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[[Category: bacteriolytic enzyme]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: lysozyme]]
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[[Category: multimodular]]
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[[Category: murein hydrolase]]
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[[Category: pneumococcal cell wall degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:07 2008''
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==See Also==
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*[[Lysin 3D structures|Lysin 3D structures]]
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus phage Cp1]]
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[[Category: Albert A]]
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[[Category: Garcia JL]]
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[[Category: Garcia P]]
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[[Category: Hermoso JA]]
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[[Category: Martinez-Ripoll M]]
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[[Category: Menendez M]]
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[[Category: Monterroso B]]

Current revision

Multimodular Pneumococcal Cell Wall Endolysin from phage Cp-1

PDB ID 1h09

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