3bcg
From Proteopedia
(Difference between revisions)
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<StructureSection load='3bcg' size='340' side='right'caption='[[3bcg]], [[Resolution|resolution]] 2.48Å' scene=''> | <StructureSection load='3bcg' size='340' side='right'caption='[[3bcg]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3bcg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3bcg]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3BCG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48Å</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=3bcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcg OCA], [https://pdbe.org/3bcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bcg RCSB], [https://www.ebi.ac.uk/pdbsum/3bcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bcg ProSAT]</span></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=3bcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcg OCA], [https://pdbe.org/3bcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bcg RCSB], [https://www.ebi.ac.uk/pdbsum/3bcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bcg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ACRR_ECOLI ACRR_ECOLI] Potential regulator protein for the acrAB genes. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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/main_output.php?pdb_ID=3bcg ConSurf]. | </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/main_output.php?pdb_ID=3bcg ConSurf]. | ||
<div style="clear:both"></div> | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3bcg" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | *[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | ||
| - | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gu | + | [[Category: Gu R]] |
| - | [[Category: Li | + | [[Category: Li M]] |
| - | [[Category: Long | + | [[Category: Long F]] |
| - | [[Category: McDermott | + | [[Category: McDermott G]] |
| - | [[Category: Su | + | [[Category: Su CC]] |
| - | [[Category: Yang | + | [[Category: Yang F]] |
| - | [[Category: Yu | + | [[Category: Yu EY]] |
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Current revision
Conformational changes of the AcrR regulator reveal a mechanism of induction
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Categories: Escherichia coli K-12 | Large Structures | Gu R | Li M | Long F | McDermott G | Su CC | Yang F | Yu EY
