3f51: Difference between revisions
m Protected "3f51" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Crystal Structure of the clp gene regulator ClgR from Corynebacterium glutamicum== | ||
<StructureSection load='3f51' size='340' side='right' caption='[[3f51]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3f51]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F51 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f52|3f52]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cg2152, Cgl1962, Clg1962 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f51 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f51 RCSB], [http://www.ebi.ac.uk/pdbsum/3f51 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human 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<ref>PMID:19019826</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Corynebacterium glutamicum]] | [[Category: Corynebacterium glutamicum]] | ||
[[Category: Bott, M | [[Category: Bott, M]] | ||
[[Category: Pohl, E | [[Category: Pohl, E]] | ||
[[Category: Polen, T | [[Category: Polen, T]] | ||
[[Category: Russo, S | [[Category: Russo, S]] | ||
[[Category: Schweitzer, J E | [[Category: Schweitzer, J E]] | ||
[[Category: Gene regulator]] | [[Category: Gene regulator]] | ||
[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
Revision as of 11:55, 26 November 2014
Crystal Structure of the clp gene regulator ClgR from Corynebacterium glutamicumCrystal Structure of the clp gene regulator ClgR from Corynebacterium glutamicum
Structural highlights
Publication 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. References
|
| ||||||||||||||||||||