3iqc: Difference between revisions

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==Crystal structure of FliS from H. pylori==
==Crystal structure of FliS from H. pylori==
<StructureSection load='3iqc' size='340' side='right' caption='[[3iqc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3iqc' size='340' side='right'caption='[[3iqc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3iqc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IQC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3iqc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IQC FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0753 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=3iqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iqc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3iqc RCSB], [http://www.ebi.ac.uk/pdbsum/3iqc PDBsum]</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=3iqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iqc OCA], [https://pdbe.org/3iqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iqc RCSB], [https://www.ebi.ac.uk/pdbsum/3iqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iqc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O25448_HELPY O25448_HELPY]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/3iqc_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/3iqc_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata 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=3iqc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3iqc" style="background-color:#fffaf0;"></div>
==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Campylobacter pylori]]
[[Category: Helicobacter pylori 26695]]
[[Category: Au, S W.N]]
[[Category: Large Structures]]
[[Category: Lam, W W.L]]
[[Category: Au SWN]]
[[Category: Ling, T K.W]]
[[Category: Lam WWL]]
[[Category: Woo, E J]]
[[Category: Ling TKW]]
[[Category: Chaperone]]
[[Category: Woo EJ]]
[[Category: Flagella]]
[[Category: Flagellum]]

Latest revision as of 19:01, 1 November 2023

Crystal structure of FliS from H. pyloriCrystal structure of FliS from H. pylori

Structural highlights

3iqc is a 2 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O25448_HELPY

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Flagellar export chaperone FliS prevents premature polymerization of flagellins and is critical for flagellar assembly and bacterial colonization. Previously, a yeast 2-hybrid study identified various FliS-associated proteins in Helicobacter pylori, but the implications of these interactions are not known. Here we demonstrate the biophysical interaction of FliS (HP0753) and the uncharacterized protein HP1076 from H. pylori. HP1076 possesses a cochaperone activity that promotes the folding and chaperone activity of FliS. We further determined the crystal structures of FliS, HP1076, and the binary complex at 2.7, 1.8, and 2.7 A resolution, respectively. HP1076 adopts a helix-rich bundle structure and interestingly shares a similar fold with a flagellin homologue, hook-associated protein, and FliS. The FliS-HP1076 complex revealed an extensive electrostatic and hydrophobic binding interface, which is distinct from the flagellin binding pocket in FliS. The helical stacking interaction between HP1076 and FliS suggests that HP1076 stabilizes 2 alpha helices of FliS and therefore the overall structure of the bundle. Our findings provide new insights into flagellar export chaperones and may have implications for other secretion chaperones in the type III secretion system.

Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori.,Lam WW, Woo EJ, Kotaka M, Tam WK, Leung YC, Ling TK, Au SW FASEB J. 2010 Oct;24(10):4020-32. doi: 10.1096/fj.10-155242. Epub 2010 Jun 25. PMID:20581225[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lam WW, Woo EJ, Kotaka M, Tam WK, Leung YC, Ling TK, Au SW. Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori. FASEB J. 2010 Oct;24(10):4020-32. doi: 10.1096/fj.10-155242. Epub 2010 Jun 25. PMID:20581225 doi:http://dx.doi.org/10.1096/fj.10-155242

3iqc, resolution 2.70Å

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OCA