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3szp

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Full-length structure of the Vibrio cholerae virulence activator, AphB, a member of the LTTR protein family

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 ==Full-length structure of the Vibrio cholerae virulence activator, AphB, a member of the LTTR protein family==
-<StructureSection load='3szp' size='340' side='right' caption='[[3szp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3szp' size='340' side='right'caption='[[3szp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3szp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SZP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3szp]] is a 2 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=3SZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZP FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t1b|3t1b]]</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]] 2.202&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC_1049 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae])</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=3szp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szp OCA], [https://pdbe.org/3szp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3szp RCSB], [https://www.ebi.ac.uk/pdbsum/3szp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3szp ProSAT]</span></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=3szp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3szp RCSB], [http://www.ebi.ac.uk/pdbsum/3szp PDBsum]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q9KT56_VIBCH Q9KT56_VIBCH]
-Expression of the two critical virulence factors of Vibrio cholerae, toxin-coregulated pilus and cholera toxin, is initiated at the tcpPH promoter by the regulators AphA and AphB. AphA is a winged helix DNA-binding protein that enhances the ability of AphB, a LysR-type transcriptional regulator, to activate tcpPH expression. We present here the 2.2 A X-ray crystal structure of full-length AphB. As reported for other LysR-type proteins, AphB is a tetramer with two distinct subunit conformations. Unlike other family members, AphB must undergo a significant conformational change in order to bind to DNA. We have found five independent mutations in the putative ligand-binding pocket region that allow AphB to constitutively activate tcpPH expression at the non-permissive pH of 8.5 and in the presence of oxygen. These findings indicate that AphB is responsive to intracellular pH as well as to anaerobiosis and that residues in the ligand-binding pocket of the protein influence its ability to respond to both of these signals. We have solved the structure of one of the constitutive mutants, and observe conformational changes that would allow DNA binding. Taken together, these results describe a pathway of conformational changes allowing communication between the ligand and DNA binding regions of AphB.
-The crystal structure of AphB, a virulence gene activator from Vibrio cholerae, reveals residues that influence its response to oxygen and pH.,Taylor JL, De Silva RS, Kovacikova G, Lin W, Taylor RK, Skorupski K, Kull FJ Mol Microbiol. 2011 Nov 7. doi: 10.1111/j.1365-2958.2011.07919.x. PMID:22053934<ref>PMID:22053934</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Vibrio cholerae]]
-[[Category: Kovacikova, G]]
+[[Category: De Silva RS]]
-[[Category: Kull, F J]]
+[[Category: Kovacikova G]]
-[[Category: Lin, W]]
+[[Category: Kull FJ]]
-[[Category: Silva, R S.De]]
+[[Category: Lin W]]
-[[Category: Skorupski, K]]
+[[Category: Skorupski K]]
-[[Category: Taylor, J L]]
+[[Category: Taylor JL]]
-[[Category: Taylor, R K]]
+[[Category: Taylor RK]]
-[[Category: Dna-binding]]
-[[Category: Transcription]]
-[[Category: Transcription factor]]
-[[Category: Winged helix-turn helix]]

3szp

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Full-length structure of the Vibrio cholerae virulence activator, AphB, a member of the LTTR protein family

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