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| | ==Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS protein from Vibrio cholerae== | | ==Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS protein from Vibrio cholerae== |
| - | <StructureSection load='1ov9' size='340' side='right' caption='[[1ov9]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='1ov9' size='340' side='right'caption='[[1ov9]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ov9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OV9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ov9]] 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=1OV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OV9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ni8|1ni8]], [[1lr1|1lr1]]</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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vich ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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=1ov9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ov9 OCA], [https://pdbe.org/1ov9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ov9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ov9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ov9 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=1ov9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ov9 OCA], [http://pdbe.org/1ov9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ov9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ov9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ov9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9KSX6_VIBCH Q9KSX6_VIBCH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillo virgola del koch trevisan 1884]] | + | [[Category: Large Structures]] |
| - | [[Category: Arold, S T]] | + | [[Category: Vibrio cholerae]] |
| - | [[Category: Bloch, V]] | + | [[Category: Arold ST]] |
| - | [[Category: Cerdan, R]] | + | [[Category: Bloch V]] |
| - | [[Category: Coiled-coil]] | + | [[Category: Cerdan R]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Helix]]
| + | |
| Structural highlights
Function
Q9KSX6_VIBCH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The histone-like nucleoid structuring (H-NS) protein is a global modulator of gene expression in Gram-negative bacteria. VicH, the H-NS protein of Vibrio cholerae, regulates the expression of certain major virulence determinants implicated in the pathogenesis of cholera. We present here the 2.5A crystal structure of the N-terminal oligomerisation domain of VicH (VicH_Nt). VicH_Nt adopts the same fold and dimeric assembly as the NMR structure of Escherichia coli H-NS_Nt, thus validating this fold against conflicting data. The structural similarity of V.cholerae VicH_Nt and E.coli H-NS_Nt, despite differences in origin, system of expression, experimental conditions and techniques used, indicates that the fold determined in our studies is robust to experimental conditions. Structural analysis and homology modelling were carried out to further elucidate the molecular basis of the functional polyvalence of the N-terminal domain. Our analysis of members of the H-NS superfamily supports the suggestion that the oligomerisation function of H-NS_Nt is conserved even in more distantly related proteins.
Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae.,Cerdan R, Bloch V, Yang Y, Bertin P, Dumas C, Rimsky S, Kochoyan M, Arold ST J Mol Biol. 2003 Nov 21;334(2):179-85. PMID:14607110[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cerdan R, Bloch V, Yang Y, Bertin P, Dumas C, Rimsky S, Kochoyan M, Arold ST. Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae. J Mol Biol. 2003 Nov 21;334(2):179-85. PMID:14607110
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