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| | <StructureSection load='5aeo' size='340' side='right'caption='[[5aeo]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5aeo' size='340' side='right'caption='[[5aeo]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5aeo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhoh1 Rhoh1]. 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> | + | <table><tr><td colspan='2'>[[5aeo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_hoagii_103S Rhodococcus hoagii 103S]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://pdbe.org/5aeo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aeo RCSB], [http://www.ebi.ac.uk/pdbsum/5aeo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aeo 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=5aeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aeo OCA], [https://pdbe.org/5aeo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aeo RCSB], [https://www.ebi.ac.uk/pdbsum/5aeo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aeo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9EU62_RHOHA Q9EU62_RHOHA] |
| | <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: Rhoh1]] | + | [[Category: Rhodococcus hoagii 103S]] |
| - | [[Category: Blagova, E V]] | + | [[Category: Blagova EV]] |
| - | [[Category: Dover, L G]] | + | [[Category: Dover LG]] |
| - | [[Category: Okoko, T]] | + | [[Category: Okoko T]] |
| - | [[Category: Whittingham, J L]] | + | [[Category: Whittingham JL]] |
| - | [[Category: Wilkinson, A J]] | + | [[Category: Wilkinson AJ]] |
| - | [[Category: Bacterial pathogen]]
| + | |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Intracellular pathogen]]
| + | |
| - | [[Category: Virulence protein]]
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| Structural highlights
Function
Q9EU62_RHOHA
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Okoko T, Blagova EV, Whittingham JL, Dover LG, Wilkinson AJ. Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi. Vet Microbiol. 2015 Feb 9. pii: S0378-1135(15)00057-7. doi:, 10.1016/j.vetmic.2015.01.027. PMID:25746683 doi:http://dx.doi.org/10.1016/j.vetmic.2015.01.027
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