3mq0: Difference between revisions
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==Crystal Structure of Agobacterium tumefaciens repressor BlcR== | |||
=== | <StructureSection load='3mq0' size='340' side='right' caption='[[3mq0]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mq0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MQ0 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGR_pAT_196, attJ, Atu5136, blcR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 Agrobacterium tumefaciens])</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=3mq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mq0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mq0 RCSB], [http://www.ebi.ac.uk/pdbsum/3mq0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Agrobacterium tumefaciens BlcR is a member of the emerging isocitrate lyase transcription regulators that negatively regulates metabolism of gamma-butyrolactone, and its repressing function is relieved by succinate semialdehyde (SSA). Our crystal structure showed that BlcR folded into the DNA- and SSA-binding domains and dimerized via the DNA-binding domains. Mutational analysis identified residues, including Phe(147), that are important for SSA association; BlcR(F147A) existed as tetramer. Two BlcR dimers bound to target DNA and in a cooperative manner, and the distance between the two BlcR-binding sequences in DNA was critical for BlcR-DNA association. Tetrameric BlcR(F147A) retained DNA binding activity, and importantly, this activity was not affected by the distance separating the BlcR-binding sequences in DNA. SSA did not dissociate tetrameric BlcR(F147A) or BlcR(F147A)-DNA. As well as in the SSA-binding site, Phe(147) is located in a structurally flexible loop that may be involved in BlcR oligomerization. We propose that SSA regulates BlcR DNA-binding function via oligomerization. | |||
The Agrobacterium tumefaciens Transcription Factor BlcR Is Regulated via Oligomerization.,Pan Y, Fiscus V, Meng W, Zheng Z, Zhang LH, Fuqua C, Chen L J Biol Chem. 2011 Jun 10;286(23):20431-40. Epub 2011 Apr 4. PMID:21467043<ref>PMID:21467043</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Agrobacterium tumefaciens]] | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: Chen, L | [[Category: Chen, L]] | ||
[[Category: Gaf fold]] | [[Category: Gaf fold]] | ||
[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
[[Category: Transcription repressor]] | [[Category: Transcription repressor]] | ||
Revision as of 16:44, 18 December 2014
Crystal Structure of Agobacterium tumefaciens repressor BlcR
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