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[[ | ==Effector binding Domain of LysR-Type transcription factor RovM from Y. pseudotuberculosis== | ||
<StructureSection load='3onm' size='340' side='right' caption='[[3onm]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3onm]] is a 2 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=3ONM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ONM FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lrhA, RovM, YpsIP31758_1452 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 Yersinia pseudotuberculosis])</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=3onm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3onm RCSB], [http://www.ebi.ac.uk/pdbsum/3onm PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4 A. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules. | |||
Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.,Quade N, Dieckmann M, Haffke M, Heroven AK, Dersch P, Heinz DW Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):81-90. Epub 2011, Jan 8. PMID:21245528<ref>PMID:21245528</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.]] | ||
Revision as of 13:30, 28 May 2014
Effector binding Domain of LysR-Type transcription factor RovM from Y. pseudotuberculosisEffector binding Domain of LysR-Type transcription factor RovM from Y. pseudotuberculosis
Structural highlights
Publication Abstract from PubMedIn enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4 A. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules. Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.,Quade N, Dieckmann M, Haffke M, Heroven AK, Dersch P, Heinz DW Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):81-90. Epub 2011, Jan 8. PMID:21245528[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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