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.

4k2e

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:33, 4 August 2016

HlyU from Vibrio cholerae N16961

Structural highlights

4k2e is a 4 chain structure with sequence from Vibch. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	hlyU, VC_0678 (VIBCH)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HLYU_VIBCH] Up-regulates the expression of the hemolysin gene, hlyA, and may promote expression of other virulence determinants in vivo. It may have both positive and negative regulator activities.

Publication Abstract from PubMed

HlyU in Vibrio cholerae is known to be the transcriptional activator of the hemolysin gene, HlyA and possibly a regulator of other virulence factors influencing growth, colonization and pathogenicity of this infective agent. Here we report the crystal structure of HlyU from V. cholerae N16961 (HlyU_Vc) at 1.8A. The protein, with five alpha-helices and three beta-strands in the topology of alpha1-alpha2-beta1-alpha3-alpha4-beta2-beta3-alpha5, forms a homodimer. Helices alpha3-alpha4 and a beta sheet form the winged helix-turn-helix (wHTH) DNA-binding motif common to the transcription regulators of the SmtB/ArsR family. In spite of an overall fold similar to SmtB/ArsR family, it lacks any metal binding site seen in SmtB. A comparison of the dimeric interfaces showed that the one in SmtB is much larger and have salt bridges that can be disrupted to accommodate metal ions. A model of HlyU-DNA complex suggests bending of the DNA. Cys38 in the structure was found to be modified as sulfenic acid; the oxidized form was not seen in another structure solved under reducing condition. Although devoid of any metal binding site, the presence of a Cys residue exhibiting oxidation-reduction suggests the possibility of the existence of a redox switch in transcription regulation. A structure-based phylogenetic analysis of wHTH proteins revealed the segregation of metal and non-metal binding proteins as well as those in the latter group that are under redox control.

Crystal structure of HlyU, the hemolysin gene transcription activator, from Vibrio cholerae N16961 and functional implications.,Mukherjee D, Datta AB, Chakrabarti P Biochim Biophys Acta. 2014 Oct 18;1844(12):2346-2354. doi:, 10.1016/j.bbapap.2014.09.020. PMID:25450504^[1]

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

References

↑ Mukherjee D, Datta AB, Chakrabarti P. Crystal structure of HlyU, the hemolysin gene transcription activator, from Vibrio cholerae N16961 and functional implications. Biochim Biophys Acta. 2014 Oct 18;1844(12):2346-2354. doi:, 10.1016/j.bbapap.2014.09.020. PMID:25450504 doi:http://dx.doi.org/10.1016/j.bbapap.2014.09.020

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4k2e"

@@ Line 1: / Line 1: @@
 ==HlyU from Vibrio cholerae N16961==
 <StructureSection load='4k2e' size='340' side='right' caption='[[4k2e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hlyU, VC_0678 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</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=4k2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k2e RCSB], [http://www.ebi.ac.uk/pdbsum/4k2e PDBsum]</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=4k2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2e OCA], [http://pdbe.org/4k2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k2e RCSB], [http://www.ebi.ac.uk/pdbsum/4k2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k2e ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4k2e" style="background-color:#fffaf0;"></div>
 ==See Also==

4k2e

From Proteopedia

Revision as of 10:33, 4 August 2016

HlyU from Vibrio cholerae N16961

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox