4k2e: Difference between revisions
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<StructureSection load='4k2e' size='340' side='right' caption='[[4k2e]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4k2e' size='340' side='right' caption='[[4k2e]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4k2e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2E OCA]. <br> | <table><tr><td colspan='2'>[[4k2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K2E FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | </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><td class="sblockLbl"><b> | <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><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://www.rcsb.org/pdb/explore.do?structureId=4k2e RCSB], [http://www.ebi.ac.uk/pdbsum/4k2e PDBsum]</span></td></tr> | ||
<table> | </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> | |||
==See Also== | |||
*[[Transcriptional activator|Transcriptional activator]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chakrabarti, P | [[Category: Vibch]] | ||
[[Category: Datta, A B | [[Category: Chakrabarti, P]] | ||
[[Category: Mukherjee, D | [[Category: Datta, A B]] | ||
[[Category: Mukherjee, D]] | |||
[[Category: Dna]] | [[Category: Dna]] | ||
[[Category: Dna-binding domain]] | [[Category: Dna-binding domain]] | ||
