4m03: Difference between revisions
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==C-terminal fragment(residues 576-751) of binding region of SraP== | ==C-terminal fragment(residues 576-751) of binding region of SraP== | ||
<StructureSection load='4m03' size='340' side='right' caption='[[4m03]], [[Resolution|resolution]] 2.24Å' scene=''> | <StructureSection load='4m03' size='340' side='right' caption='[[4m03]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m00|4m00]], [[4m01|4m01]], [[4m02|4m02]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m00|4m00]], [[4m01|4m01]], [[4m02|4m02]]</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=4m03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m03 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m03 RCSB], [http://www.ebi.ac.uk/pdbsum/4m03 PDBsum]</span></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=4m03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m03 OCA], [http://pdbe.org/4m03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m03 RCSB], [http://www.ebi.ac.uk/pdbsum/4m03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m03 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4m03" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 23:35, 5 August 2016
C-terminal fragment(residues 576-751) of binding region of SraPC-terminal fragment(residues 576-751) of binding region of SraP
Structural highlights
Function[SRAP_STAA8] Mediates binding to human platelets, possibly through a receptor-ligand interaction. Probably associated with virulence in endovascular infection.[1] Publication Abstract from PubMedStaphylococcus aureus, a Gram-positive bacterium causes a number of devastating human diseases, such as infective endocarditis, osteomyelitis, septic arthritis and sepsis. S. aureus SraP, a surface-exposed serine-rich repeat glycoprotein (SRRP), is required for the pathogenesis of human infective endocarditis via its ligand-binding region (BR) adhering to human platelets. It remains unclear how SraP interacts with human host. Here we report the 2.05 A crystal structure of the BR of SraP, revealing an extended rod-like architecture of four discrete modules. The N-terminal legume lectin-like module specifically binds to N-acetylneuraminic acid. The second module adopts a beta-grasp fold similar to Ig-binding proteins, whereas the last two tandem repetitive modules resemble eukaryotic cadherins but differ in calcium coordination pattern. Under the conditions tested, small-angle X-ray scattering and molecular dynamic simulation indicated that the three C-terminal modules function as a relatively rigid stem to extend the N-terminal lectin module outwards. Structure-guided mutagenesis analyses, in addition to a recently identified trisaccharide ligand of SraP, enabled us to elucidate that SraP binding to sialylated receptors promotes S. aureus adhesion to and invasion into host epithelial cells. Our findings have thus provided novel structural and functional insights into the SraP-mediated host-pathogen interaction of S. aureus. Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells.,Yang YH, Jiang YL, Zhang J, Wang L, Bai XH, Zhang SJ, Ren YM, Li N, Zhang YH, Zhang Z, Gong Q, Mei Y, Xue T, Zhang JR, Chen Y, Zhou CZ PLoS Pathog. 2014 Jun 5;10(6):e1004169. doi: 10.1371/journal.ppat.1004169., eCollection 2014 Jun. PMID:24901708[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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