4ooi
From Proteopedia
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| - | ''' | + | ==Reduced HlyU from Vibrio cholerae N16961== |
| + | <StructureSection load='4ooi' size='340' side='right' caption='[[4ooi]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ooi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OOI FirstGlance]. <br> | ||
| + | </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=4ooi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ooi RCSB], [http://www.ebi.ac.uk/pdbsum/4ooi PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HLYU_VIBCH 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25450504</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Chakrabarti, P]] | [[Category: Chakrabarti, P]] | ||
| - | [[Category: Datta, A | + | [[Category: Datta, A B]] |
[[Category: Mukherjee, D]] | [[Category: Mukherjee, D]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Dna-binding domain]] | ||
| + | [[Category: Hemolysin gene transcription regulator]] | ||
| + | [[Category: Winged helix]] | ||
Revision as of 14:44, 31 December 2014
Reduced HlyU from Vibrio cholerae N16961
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