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6ceq

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Current revision (14:27, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6ceq' size='340' side='right'caption='[[6ceq]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='6ceq' size='340' side='right'caption='[[6ceq]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ceq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CEQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ceq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CEQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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]] 1.67&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSW01_19535 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<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=6ceq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ceq OCA], [http://pdbe.org/6ceq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ceq RCSB], [http://www.ebi.ac.uk/pdbsum/6ceq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ceq ProSAT]</span></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=6ceq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ceq OCA], [https://pdbe.org/6ceq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ceq RCSB], [https://www.ebi.ac.uk/pdbsum/6ceq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ceq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9KKL2_VIBCH Q9KKL2_VIBCH]
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The diarrheal pathogen Vibrio cholerae navigates complex environments using three chemosensory systems and 44-45 chemoreceptors. Chemosensory cluster II modulates chemotaxis, whereas clusters I and III have unknown functions. Ligands have been identified for only five V. cholerae chemoreceptors. Here we report that the cluster III receptor, VcAer2, binds and responds to O2 . VcAer2 is an ortholog of Pseudomonas aeruginosa Aer2 (PaAer2), but differs in that VcAer2 has two, rather than one, N-terminal PAS domain. We have determined that both PAS1 and PAS2 form homodimers and bind penta-coordinate b-type heme via an Eeta-His residue. Heme binding to PAS1 required the entire PAS core, but receptor function also required the N-terminal cap. PAS2 functioned as an O2 -sensor [Kd(O2) , 19 muM], utilizing the same Ibeta Trp (W276) as PaAer2 to stabilize O2 . The crystal structure of PAS2-W276L was similar to that of PaAer2-PAS, but resided in an active conformation mimicking the ligand-bound state, consistent with its signal-on phenotype. PAS1 also bound O2 [Kd(O2), 12 muM], although O2 binding was stabilized by either a Trp or Tyr residue. Moreover, PAS1 appeared to function as a signal modulator, regulating O2 -mediated signaling from PAS2, and resulting in activation of the cluster III chemosensory pathway. This article is protected by copyright. All rights reserved.
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THE AER2 RECEPTOR FROM VIBRIO CHOLERAE IS A DUAL PAS-HEME OXYGEN SENSOR.,Greer-Phillips SE, Sukomon N, Chua TK, Johnson MS, Crane BR, Watts KJ Mol Microbiol. 2018 May 2. doi: 10.1111/mmi.13978. PMID:29719085<ref>PMID:29719085</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 6ceq" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillo virgola del koch trevisan 1884]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chua, T K]]
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[[Category: Vibrio cholerae]]
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[[Category: Crane, B R]]
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[[Category: Chua TK]]
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[[Category: Sukomon, N]]
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[[Category: Crane BR]]
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[[Category: Chemoreceptor]]
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[[Category: Sukomon N]]
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[[Category: Heme]]
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[[Category: Pas domain]]
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[[Category: Signal transduction]]
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[[Category: Signaling protein]]
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[[Category: Vibrio cholera]]
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Current revision

The Aer2 Receptor from Vibrio cholerae is a Dual PAS-Heme Oxygen Sensor

PDB ID 6ceq

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