2yvh: Difference between revisions

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<StructureSection load='2yvh' size='340' side='right'caption='[[2yvh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2yvh' size='340' side='right'caption='[[2yvh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2yvh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Corgl Corgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YVH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2yvh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YVH FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zoy|2zoy]], [[2zoz|2zoz]], [[2yve|2yve]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cgl2612 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=196627 CORGL])</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=2yvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvh OCA], [https://pdbe.org/2yvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yvh RCSB], [https://www.ebi.ac.uk/pdbsum/2yvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yvh 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=2yvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvh OCA], [https://pdbe.org/2yvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yvh RCSB], [https://www.ebi.ac.uk/pdbsum/2yvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yvh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8NMG3_CORGL Q8NMG3_CORGL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/2yvh_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/2yvh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 2yvh" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2yvh" style="background-color:#fffaf0;"></div>
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Corgl]]
[[Category: Corynebacterium glutamicum ATCC 13032]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Itou, H]]
[[Category: Itou H]]
[[Category: Shirakihara, Y]]
[[Category: Shirakihara Y]]
[[Category: Tanaka, I]]
[[Category: Tanaka I]]
[[Category: Helix-turn-helix]]
[[Category: Protein-dna complex]]
[[Category: Tetr-family]]
[[Category: Transcription-dna complex]]

Latest revision as of 11:07, 23 October 2024

Crystal structure of the operator-binding form of the multi-drug binding transcriptional repressor CgmRCrystal structure of the operator-binding form of the multi-drug binding transcriptional repressor CgmR

Structural highlights

2yvh is a 8 chain structure with sequence from Corynebacterium glutamicum ATCC 13032. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8NMG3_CORGL

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 PubMed

CgmR (CGL2612) from Corynebacterium glutamicum is a multidrug-resistance-related transcription factor belonging to the TetR family, which is a protein family of widespread bacterial transcription factors typically involved in environmental response. Here, we report the crystal structures of CgmR homodimeric repressor in complex with two distinct inducers (1.95 and 1.4 A resolution) and with an operator (2.5 A resolution). The CgmR-operator complex showed that two CgmR dimers bound to the operator, and each half-site of the palindromic operator was asymmetrically recognized by two DNA-binding domains from different dimers on the opposite sides of the DNA. The inducer complexes demonstrated that both bound inducers act as a wedge to alter the operator-binding conformation of the repressor by steric inhibition. As steric hindrance is used, various drugs should act as inducers if they have sufficient volume for the conformation change and if their bindings sufficiently reduce free energy. The comparative structural study of CgmR free protein, in complex with operator, and with inducers, implies the other mechanism that might contribute to multidrug response of the repressor.

Crystal Structures of the Multidrug Binding Repressor Corynebacteriumglutamicum CgmR in Complex with Inducers and with an Operator.,Itou H, Watanabe N, Yao M, Shirakihara Y, Tanaka I J Mol Biol. 2010 Aug 5. PMID:20691702[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Itou H, Watanabe N, Yao M, Shirakihara Y, Tanaka I. Crystal Structures of the Multidrug Binding Repressor Corynebacteriumglutamicum CgmR in Complex with Inducers and with an Operator. J Mol Biol. 2010 Aug 5. PMID:20691702 doi:10.1016/j.jmb.2010.07.042

2yvh, resolution 2.50Å

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OCA