1o9y

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<StructureSection load='1o9y' size='340' side='right'caption='[[1o9y]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='1o9y' size='340' side='right'caption='[[1o9y]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1o9y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O9Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1o9y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O9Y FirstGlance]. <br>
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</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=1o9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9y OCA], [https://pdbe.org/1o9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o9y RCSB], [https://www.ebi.ac.uk/pdbsum/1o9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o9y ProSAT]</span></td></tr>
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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]] 2.29&#8491;</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=1o9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9y OCA], [https://pdbe.org/1o9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o9y RCSB], [https://www.ebi.ac.uk/pdbsum/1o9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o9y ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HRCQB_PSESH HRCQB_PSESH] Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with HrcQa.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o9y ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o9y ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Type III secretion systems enable plant and animal bacterial pathogens to deliver virulence proteins into the cytosol of eukaryotic host cells, causing a broad spectrum of diseases including bacteremia, septicemia, typhoid fever, and bubonic plague in mammals, and localized lesions, systemic wilting, and blights in plants. In addition, type III secretion systems are also required for biogenesis of the bacterial flagellum. The HrcQ(B) protein, a component of the secretion apparatus of Pseudomonas syringae with homologues in all type III systems, has a variable N-terminal and a conserved C-terminal domain (HrcQ(B)-C). Here, we report the crystal structure of HrcQ(B)-C and show that this domain retains the ability of the full-length protein to interact with other type III components. A 3D analysis of sequence conservation patterns reveals two clusters of residues potentially involved in protein-protein interactions. Based on the analogies between HrcQ(B) and its flagellum homologues, we propose that HrcQ(B)-C participates in the formation of a C-ring-like assembly.
 
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Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems.,Fadouloglou VE, Tampakaki AP, Glykos NM, Bastaki MN, Hadden JM, Phillips SE, Panopoulos NJ, Kokkinidis M Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):70-5. Epub 2003 Dec 23. PMID:14694203<ref>PMID:14694203</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1o9y" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 19310]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fadouloglou, V E]]
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[[Category: Pseudomonas syringae]]
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[[Category: Kokkinidis, M]]
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[[Category: Fadouloglou VE]]
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[[Category: Hrp]]
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[[Category: Kokkinidis M]]
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[[Category: Phytopathogenicity]]
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[[Category: Secretory protein]]
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[[Category: Structural protein]]
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[[Category: Type iii secretion system]]
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Revision as of 08:56, 10 April 2024

Crystal structure of the C-terminal domain of the HrcQb protein from Pseudomonas syringae pv. phaseolicola

PDB ID 1o9y

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