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| | <StructureSection load='1h09' size='340' side='right'caption='[[1h09]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1h09' size='340' side='right'caption='[[1h09]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h09]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpcp1 Bpcp1]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H09 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1h09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h09 RCSB], [http://www.ebi.ac.uk/pdbsum/1h09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h09 ProSAT]</span></td></tr> | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Lysin|Lysin]] | + | *[[Lysin 3D structures|Lysin 3D structures]] |
| | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpcp1]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]] | + | [[Category: Streptococcus phage Cp1]] |
| - | [[Category: Albert, A]] | + | [[Category: Albert A]] |
| - | [[Category: Garcia, J L]] | + | [[Category: Garcia JL]] |
| - | [[Category: Garcia, P]] | + | [[Category: Garcia P]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Martinez-Ripoll, M]] | + | [[Category: Martinez-Ripoll M]] |
| - | [[Category: Menendez, M]] | + | [[Category: Menendez M]] |
| - | [[Category: Monterroso, B]] | + | [[Category: Monterroso B]] |
| - | [[Category: Bacteriolytic enzyme]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Multimodular]]
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| - | [[Category: Murein hydrolase]]
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| - | [[Category: Pneumococcal cell wall degradation]]
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| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Structure. 2003 Oct;11(10):1239-49. PMID:14527392
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