5aeo: Difference between revisions
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''' | ==Virulence-associated protein VapG from the intracellular pathogen Rhodococcus equi== | ||
<StructureSection load='5aeo' size='340' side='right' caption='[[5aeo]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5aeo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AEO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=5aeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aeo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aeo RCSB], [http://www.ebi.ac.uk/pdbsum/5aeo PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Virulence and host range in Rhodococcus equi depends on the variable pathogenicity island of their virulence plasmids. Notable gene products are a family of small secreted virulence-associated proteins (Vaps) that are critical to intramacrophagic proliferation. Equine-adapted strains, which cause severe pyogranulomatous pneumonia in foals, produce a cell-associated VapA that is necessary for virulence, alongside five other secreted homologues. In the absence of biochemical insight, attention has turned to the structures of these proteins to develop a functional hypothesis. Recent studies have described crystal structures for VapD and a truncate of the VapA orthologue of porcine-adapted strains, VapB. Here, we crystallised the full-length VapG and determined its structure by molecular replacement. Electron density corresponding to the N-terminal domain was not visible suggesting that it is disordered. The protein core adopted a compact elliptical, anti-parallel beta-barrel fold with beta1-beta2-beta3-beta8-beta5-beta6-beta7-beta4 topology decorated by a single peripheral alpha-helix unique to this family. The high glycine content of the protein allows close packing of secondary structural elements. Topologically, the surface has no indentations that indicate a nexus for molecular interactions. The distribution of polar and apolar groups on the surface of VapG is markedly uneven. One-third of the surface is dominated by exposed apolar side-chains, with no ionisable and only four polar side-chains exposed, giving rise to an expansive flat hydrophobic surface. Other surface regions are more polar, especially on or near the alpha-helix and a belt around the centre of the beta-barrel. Possible functional significance of these recent structures is discussed. | |||
Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.,Okoko T, Blagova EV, Whittingham JL, Dover LG, Wilkinson AJ Vet Microbiol. 2015 Feb 9. pii: S0378-1135(15)00057-7. doi:, 10.1016/j.vetmic.2015.01.027. PMID:25746683<ref>PMID:25746683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Blagova, E V]] | ||
[[Category: Dover, L G]] | |||
[[Category: Okoko, T]] | [[Category: Okoko, T]] | ||
[[Category: | [[Category: Whittingham, J L]] | ||
[[Category: Wilkinson, A J]] | |||
[[Category: Bacterial pathogen]] | |||
[[Category: Beta barrel]] | |||
[[Category: Immune system]] | |||
[[Category: Intracellular pathogen]] | |||
[[Category: Virulence protein]] | |||
