4mr0: Difference between revisions
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==Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae== | |||
<StructureSection load='4mr0' size='340' side='right' caption='[[4mr0]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mr0]] is a 2 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=4MR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MR0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pfbA, spr1652 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 STRR6])</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=4mr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mr0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mr0 RCSB], [http://www.ebi.ac.uk/pdbsum/4mr0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
PfbA is a surface adhesin and invasin of Streptococcus pneumoniae that binds to human fibronectin and plasminogen of the host extracellular matrix. It is a virulence factor for its pathogenesis. The crystal structure of recombinant PfbA150-607 from S. pneumoniae strain R6, was determined using multiwavelength anomalous dispersion (MAD) method and refined to 1.90A resolution. The structure of rPfbA150-607 revealed that residues Thr150 to Lys570 form a rigid parallel beta helix, followed by a short disordered region (571-607) that consists of beta hairpins. The structural organization of the beta helix resembles that of polysaccharide-modifying enzymes. The structural and sequence features essential for fibronectin-binding observed in the well characterized fibronectin-binding proteins such as FnBPA of Staphylococcus aureus, SfbI of Streptococcus pyogenes and BBK32 of Borrelia burgdorferi has been found in rPfbA150-607. Based on this, it is predicted that the disordered region following the beta helix could be the fibronectin-binding region in PfbA. PfbA150-607 contains relatively high number of surface exposed lysines and these residues are probably involved in binding plasmin(ogen) as observed in other plasminogen-binding proteins. | |||
Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae, provides hints into its interaction with fibronectin.,Beulin DS, Yamaguchi M, Kawabata S, Ponnuraj K Int J Biol Macromol. 2013 Dec 7;64C:168-173. doi: 10.1016/j.ijbiomac.2013.11.035. PMID:24321492<ref>PMID:24321492</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
[[Category: Beulin, D S.J | </StructureSection> | ||
[[Category: Ponnuraj, K | [[Category: Strr6]] | ||
[[Category: Beulin, D S.J]] | |||
[[Category: Ponnuraj, K]] | |||
[[Category: Adhesion]] | [[Category: Adhesion]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
Revision as of 18:34, 21 December 2014
Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae
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