This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3t1b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:14, 14 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of the full-length AphB N100E variant==
==Crystal structure of the full-length AphB N100E variant==
-
<StructureSection load='3t1b' size='340' side='right' caption='[[3t1b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+
<StructureSection load='3t1b' size='340' side='right'caption='[[3t1b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3t1b]] is a 4 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=3T1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T1B FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3t1b]] is a 4 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=3T1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T1B FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3szp|3szp]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aphB, 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=3t1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1b OCA], [https://pdbe.org/3t1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t1b RCSB], [https://www.ebi.ac.uk/pdbsum/3t1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1b 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=3t1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t1b RCSB], [http://www.ebi.ac.uk/pdbsum/3t1b PDBsum]</span></td></tr>
+
</table>
</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__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[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: Transcription]]
+
-
[[Category: Virulence]]
+
-
[[Category: Winged helix]]
+

Current revision

Crystal structure of the full-length AphB N100E variant

PDB ID 3t1b

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3t1b"
Personal tools