5dza

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'''Unreleased structure'''
 
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The entry 5dza is ON HOLD
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==Streptococcus agalactiae AgI/II polypeptide BspA C terminal domain (WT)==
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<StructureSection load='5dza' size='340' side='right'caption='[[5dza]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.19&#8491;</td></tr>
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<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>
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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=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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Rego, S., Till, M., Race, P.R.
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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<ref>PMID:27311712</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Race, P.R]]
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<div class="pdbe-citations 5dza" style="background-color:#fffaf0;"></div>
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[[Category: Rego, S]]
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== References ==
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[[Category: Till, M]]
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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 agalactiae NEM316]]
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[[Category: Race PR]]
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[[Category: Rego S]]
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[[Category: Till M]]

Current revision

Streptococcus agalactiae AgI/II polypeptide BspA C terminal domain (WT)

PDB ID 5dza

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