1ixc: Difference between revisions
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<StructureSection load='1ixc' size='340' side='right'caption='[[1ixc]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1ixc' size='340' side='right'caption='[[1ixc]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ixc]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ixc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IXC 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]] 2.2Å</td></tr> | ||
<tr id=' | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ixc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ixc OCA], [https://pdbe.org/1ixc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ixc RCSB], [https://www.ebi.ac.uk/pdbsum/1ixc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ixc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9WXC7_CUPNE Q9WXC7_CUPNE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 1ixc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1ixc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cupriavidus necator]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Miyashita | [[Category: Miyashita K]] | ||
[[Category: Muraoka | [[Category: Muraoka S]] | ||
[[Category: Ogawa | [[Category: Ogawa N]] | ||
[[Category: Okumura | [[Category: Okumura R]] | ||
[[Category: Senda | [[Category: Senda T]] | ||
Revision as of 02:38, 28 December 2023
Crystal structure of CbnR, a LysR family transcriptional regulatorCrystal structure of CbnR, a LysR family transcriptional regulator
Structural highlights
FunctionEvolutionary 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 LysR-type transcriptional regulator (LTTR) proteins are one of the most common transcriptional regulators in prokaryotes. Here we report the crystal structure of CbnR, which is one of the LTTRs derived from Ralstonia eutropha NH9. This is the first crystal structure of a full-length LTTR. CbnR was found to form a homo-tetramer, which seems to be a biologically active form. Surprisingly, the tetramer can be regarded as a dimer of dimers, whereby each dimer is composed of two subunits in different conformations. In the CbnR tetramer, the DNA-binding domains are located at the V-shaped bottom of the main body of the tetramer, and seem to be suitable to interact with a long stretch of the promoter DNA, which is approximately 60bp. Interaction between the four DNA-binding domains and the two binding sites on the target DNA is likely to bend the target DNA along the V-shaped bottom of the CbnR tetramer. The relaxation of the bent DNA, which occurs upon inducer binding to CbnR, seems to be associated with a quaternary structure change of the tetramer. Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend.,Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T J Mol Biol. 2003 May 2;328(3):555-66. PMID:12706716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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