3f52: Difference between revisions
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<StructureSection load='3f52' size='340' side='right'caption='[[3f52]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='3f52' size='340' side='right'caption='[[3f52]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3f52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3f52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F52 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]] 1.75Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3f52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f52 OCA], [https://pdbe.org/3f52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f52 RCSB], [https://www.ebi.ac.uk/pdbsum/3f52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f52 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=3f52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f52 OCA], [https://pdbe.org/3f52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f52 RCSB], [https://www.ebi.ac.uk/pdbsum/3f52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8NP59_CORGL Q8NP59_CORGL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3f52" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3f52" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Corynebacterium glutamicum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bott | [[Category: Bott M]] | ||
[[Category: Pohl | [[Category: Pohl E]] | ||
[[Category: Polen | [[Category: Polen T]] | ||
[[Category: Russo | [[Category: Russo S]] | ||
[[Category: Schweitzer | [[Category: Schweitzer JE]] | ||
Latest revision as of 09:42, 6 September 2023
Crystal structure of the clp gene regulator ClgR from C. glutamicumCrystal structure of the clp gene regulator ClgR from C. glutamicum
Structural highlights
FunctionPublication Abstract from PubMedHuman pathogens of the genera Corynebacterium and Mycobacterium possess the transcriptional activator ClgR (clp gene regulator) which in Corynebacterium glutamicum has been shown to regulate the expression of the ClpCP protease genes. ClgR specifically binds to pseudo-palindromic operator regions upstream of clpC and clpP1P2. Here, we present the first crystal structure of a ClgR protein from C. glutamicum. The structure was determined from two different crystal forms to resolutions of 1.75 and 2.05 A, respectively. ClgR folds into a five-helix bundle with a helix-turn-helix motif typical for DNA-binding proteins. Upon dimerization the two DNA-recognition helices are arranged opposite to each other at the protein surface in a distance of approximately 30 A, which suggests that they bind into two adjacent major grooves of B-DNA in an anti-parallel manner. A binding pocket is situated at a strategic position in the dimer interface and could possess a regulatory role altering the positions of the DNA-binding helices. Crystal structure of the caseinolytic protease gene regulator, a transcriptional activator in actinomycetes.,Russo S, Schweitzer JE, Polen T, Bott M, Pohl E J Biol Chem. 2009 Feb 20;284(8):5208-16. Epub 2008 Nov 19. PMID:19019826[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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