3bcg: Difference between revisions
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[[Image: | ==Conformational changes of the AcrR regulator reveal a mechanism of induction== | ||
<StructureSection load='3bcg' size='340' side='right' caption='[[3bcg]], [[Resolution|resolution]] 2.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3bcg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BCG FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=3bcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bcg RCSB], [http://www.ebi.ac.uk/pdbsum/3bcg PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/3bcg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Escherichia coli AcrR multidrug-binding protein represses transcription of acrAB and is induced by many structurally unrelated cytotoxic compounds. The crystal structure of AcrR in space group P222(1) has been reported previously. This P222(1) structure has provided direct information about the multidrug-binding site and important residues for drug recognition. Here, a crystal structure of this regulator in space group P3(1) is presented. Comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation. | |||
Conformational change of the AcrR regulator reveals a possible mechanism of induction.,Gu R, Li M, Su CC, Long F, Routh MD, Yang F, McDermott G, Yu EW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt, 7):584-8. Epub 2008 Jun 11. PMID:18607081<ref>PMID:18607081</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Gu, R.]] | [[Category: Gu, R.]] |
Revision as of 00:32, 3 October 2014
Conformational changes of the AcrR regulator reveal a mechanism of inductionConformational changes of the AcrR regulator reveal a mechanism of induction
Structural highlights
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 PubMedThe Escherichia coli AcrR multidrug-binding protein represses transcription of acrAB and is induced by many structurally unrelated cytotoxic compounds. The crystal structure of AcrR in space group P222(1) has been reported previously. This P222(1) structure has provided direct information about the multidrug-binding site and important residues for drug recognition. Here, a crystal structure of this regulator in space group P3(1) is presented. Comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation. Conformational change of the AcrR regulator reveals a possible mechanism of induction.,Gu R, Li M, Su CC, Long F, Routh MD, Yang F, McDermott G, Yu EW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt, 7):584-8. Epub 2008 Jun 11. PMID:18607081[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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