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| | <StructureSection load='5dza' size='340' side='right'caption='[[5dza]], [[Resolution|resolution]] 2.19Å' scene=''> | | <StructureSection load='5dza' size='340' side='right'caption='[[5dza]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dza]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Stra3 Stra3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DZA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dza]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_NEM316 Streptococcus agalactiae NEM316]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DZA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.19Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gbs1143 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211110 STRA3])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5dza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dza OCA], [http://pdbe.org/5dza PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dza RCSB], [http://www.ebi.ac.uk/pdbsum/5dza PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dza 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=5dza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dza OCA], [https://pdbe.org/5dza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dza RCSB], [https://www.ebi.ac.uk/pdbsum/5dza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dza ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8E589_STRA3 Q8E589_STRA3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Stra3]] | + | [[Category: Streptococcus agalactiae NEM316]] |
| - | [[Category: Race, P R]] | + | [[Category: Race PR]] |
| - | [[Category: Rego, S]] | + | [[Category: Rego S]] |
| - | [[Category: Till, M]] | + | [[Category: Till M]] |
| - | [[Category: Adhesin]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| Structural highlights
Function
Q8E589_STRA3
Publication Abstract from PubMed
Streptococcus agalactiae (Group B Streptococcus, GBS) is the predominant cause of early-onset infectious disease in neonates and is responsible for life threatening infections in elderly and immune-compromised individuals. Clinical manifestations of GBS infection include sepsis, pneumonia and meningitis. Here we describe BspA, a deviant antigen I/II family polypeptide that confers adhesive properties linked to pathogenesis in GBS. Heterologous expression of BspA on the surface of the non-adherent bacterium Lactococcus lactis confers adherence to scavenger receptor gp340, human vaginal epithelium, and to the fungus Candida albicans Complementary crystallographic and biophysical characterization of BspA reveal a novel beta-sandwich adhesion domain and unique asparagine-dependent super-helical stalk. Collectively these findings establish a new bacterial adhesin structure that has in effect been hijacked by a pathogenic Streptococcus species to provide competitive advantage in human mucosal infections.
Structural and Functional Analysis of Cell Wall-Anchored Polypeptide Adhesin BspA in Streptococcus agalactiae.,Rego S, Heal TJ, Pidwill GR, Till M, Robson A, Lamont RJ, Sessions RB, Jenkinson HF, Race PR, Nobbs AH J Biol Chem. 2016 Jun 15. pii: jbc.M116.726562. PMID:27311712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rego S, Heal TJ, Pidwill GR, Till M, Robson A, Lamont RJ, Sessions RB, Jenkinson HF, Race PR, Nobbs AH. Structural and Functional Analysis of Cell Wall-Anchored Polypeptide Adhesin BspA in Streptococcus agalactiae. J Biol Chem. 2016 Jun 15. pii: jbc.M116.726562. PMID:27311712 doi:http://dx.doi.org/10.1074/jbc.M116.726562
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