3tu3: Difference between revisions
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==1.92 Angstrom resolution crystal structure of the full-length SpcU in complex with full-length ExoU from the type III secretion system of Pseudomonas aeruginosa== | ==1.92 Angstrom resolution crystal structure of the full-length SpcU in complex with full-length ExoU from the type III secretion system of Pseudomonas aeruginosa== | ||
<StructureSection load='3tu3' size='340' side='right' caption='[[3tu3]], [[Resolution|resolution]] 1.92Å' scene=''> | <StructureSection load='3tu3' size='340' side='right'caption='[[3tu3]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tu3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tu3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TU3 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXA77, EXC3, RS15, spcU ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXA77, EXC3, RS15, spcU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885]), EXC2, exoU, pepA, RS14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu3 OCA], [https://pdbe.org/3tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/3tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Anderson, W F]] | [[Category: Anderson, W F]] | ||
[[Category: Borek, D]] | [[Category: Borek, D]] | ||
Revision as of 08:45, 13 July 2022
1.92 Angstrom resolution crystal structure of the full-length SpcU in complex with full-length ExoU from the type III secretion system of Pseudomonas aeruginosa1.92 Angstrom resolution crystal structure of the full-length SpcU in complex with full-length ExoU from the type III secretion system of Pseudomonas aeruginosa
Structural highlights
Publication Abstract from PubMedDisease causing bacteria often manipulate host cells in a way that facilitates the infectious process. Many pathogenic gram-negative bacteria accomplish this by using type III secretion systems. In these complex secretion pathways, bacterial chaperones direct effector proteins to a needle-like secretion apparatus, which then delivers the effector protein into the host cell cytosol. The effector protein ExoU and its chaperone SpcU are components of the Pseudomonas aeruginosa type III secretion system. Secretion of ExoU has been associated with more severe infections in both humans and animal models. Here we describe the 1.92 A X-ray structure of the ExoU-SpcU complex, a full-length type III effector in complex with its full-length cognate chaperone. Our crystallographic data allow a better understanding of the mechanism by which ExoU kills host cells and provides a foundation for future studies aimed at designing inhibitors of this potent toxin. Structure of the Type III Secretion Effector Protein ExoU in Complex with Its Chaperone SpcU.,Halavaty AS, Borek D, Tyson GH, Veesenmeyer JL, Shuvalova L, Minasov G, Otwinowski Z, Hauser AR, Anderson WF PLoS One. 2012;7(11):e49388. doi: 10.1371/journal.pone.0049388. Epub 2012 Nov 14. PMID:23166655[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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