4aik: Difference between revisions
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[[ | ==Crystal structure of RovA from Yersinia in complex with an invasin promoter fragment== | ||
<StructureSection load='4aik' size='340' side='right' caption='[[4aik]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4aik]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AIK FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aih|4aih]], [[4aij|4aij]]</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=4aik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aik OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aik RCSB], [http://www.ebi.ac.uk/pdbsum/4aik PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pathogens often rely on thermosensing to adjust virulence gene expression. In yersiniae, important virulence-associated traits are under the control of the master regulator RovA which uses an in-built thermosensor to control its activity. Thermal upshifts encountered upon host entry induce conformational changes of the RovA dimer that attenuate DNA-binding and render the protein more susceptible to proteolysis. Here, we report the crystal structure of RovA in the free and DNA-bound form and provide evidence that thermo-induced loss of RovA activity is mainly promoted by a thermosensing loop in the dimerization domain and residues in the adjacent C-terminal helix. These determinants allow partial unfolding of the regulator upon an upshift to 37 degrees C. This structural distortion is transmitted to the flexible DNA-binding domain of RovA. RovA mainly contacts the DNA backbone in a low affinity-binding mode which allows the immediate release of RovA from its operator sites. We also show that SlyA, a close homologue of RovA from Salmonella with a very similar structure, is not a thermosensor and remains active and stable at 37 degrees C. Strikingly, changes in only three amino acids, reflecting evolutionary replacements in SlyA, result in a complete loss of the thermosensing properties of RovA and prevent degradation. In conclusion, only minor alterations can transform a thermotolerant regulator into a thermosensor that allows adjustment of virulence and fitness determinants to their thermal environment. | |||
Structural basis for intrinsic thermosensing by the master virulence regulator RovA of Yersinia.,Quade N, Mendonca C, Herbst K, Heroven AK, Ritter C, Heinz DW, Dersch P J Biol Chem. 2012 Aug 30. PMID:22936808<ref>PMID:22936808</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Yersinia pseudotuberculosis]] | [[Category: Yersinia pseudotuberculosis]] | ||
[[Category: Dersch, P | [[Category: Dersch, P]] | ||
[[Category: Heinz, D W | [[Category: Heinz, D W]] | ||
[[Category: Herbst, K | [[Category: Herbst, K]] | ||
[[Category: Heroven, A K | [[Category: Heroven, A K]] | ||
[[Category: Mendonca, C | [[Category: Mendonca, C]] | ||
[[Category: Quade, N | [[Category: Quade, N]] | ||
[[Category: Global regulator]] | [[Category: Global regulator]] | ||
[[Category: Thermosensing]] | [[Category: Thermosensing]] | ||
