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| | ==CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE== | | ==CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE== |
| - | <StructureSection load='2v04' size='340' side='right' caption='[[2v04]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2v04' size='340' side='right'caption='[[2v04]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v04]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V04 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v04]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V04 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v05|2v05]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene></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=2v04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v04 OCA], [http://pdbe.org/2v04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v04 RCSB], [http://www.ebi.ac.uk/pdbsum/2v04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v04 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=2v04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v04 OCA], [https://pdbe.org/2v04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v04 RCSB], [https://www.ebi.ac.uk/pdbsum/2v04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v04 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8DR52_STRR6 Q8DR52_STRR6] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strr6]] | + | [[Category: Large Structures]] |
| - | [[Category: Hermoso, J]] | + | [[Category: Streptococcus pneumoniae R6]] |
| - | [[Category: Kahn, R]] | + | [[Category: Hermoso J]] |
| - | [[Category: Molina, R]] | + | [[Category: Kahn R]] |
| - | [[Category: Stelter, M]] | + | [[Category: Molina R]] |
| - | [[Category: Cbpf]]
| + | [[Category: Stelter M]] |
| - | [[Category: Choline-binding-protein]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Lipid-binding-protein]]
| + | |
| Structural highlights
Function
Q8DR52_STRR6
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
Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline-binding proteins. The three-dimensional structure of choline-binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non-consensus choline-binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well-defined modules. The carboxy-terminal module is involved in cell wall binding and the amino-terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis.
Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae.,Molina R, Gonzalez A, Stelter M, Perez-Dorado I, Kahn R, Morales M, Moscoso M, Campuzano S, Campillo NE, Mobashery S, Garcia JL, Garcia P, Hermoso JA EMBO Rep. 2009 Mar;10(3):246-51. Epub 2009 Jan 23. PMID:19165143[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Molina R, Gonzalez A, Stelter M, Perez-Dorado I, Kahn R, Morales M, Moscoso M, Campuzano S, Campillo NE, Mobashery S, Garcia JL, Garcia P, Hermoso JA. Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae. EMBO Rep. 2009 Mar;10(3):246-51. Epub 2009 Jan 23. PMID:19165143 doi:10.1038/embor.2008.245
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