3ere
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of the arginine repressor protein from Mycobacterium tuberculosis in complex with the DNA operator== | |
| - | + | <StructureSection load='3ere' size='340' side='right' caption='[[3ere]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3ere]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ERE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ERE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bue|3bue]], [[2zfz|2zfz]], [[3cag|3cag]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argR, ahrC, Rv1657, MT1695, MTCY06H11.22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</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=3ere FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ere OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ere RCSB], [http://www.ebi.ac.uk/pdbsum/3ere PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/3ere_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The arginine repressor (ArgR) from Mycobacterium tuberculosis (Mtb) is a gene product encoded by the open reading frame Rv1657. It regulates the L-arginine concentration in cells by interacting with ARG boxes in the promoter regions of the arginine biosynthesis and catabolism operons. Here we present a 2.5-A structure of MtbArgR in complex with a 16-bp DNA operator in the absence of arginine. A biological trimer of the protein-DNA complex is formed via the crystallographic 3-fold symmetry axis. The N-terminal domain of MtbArgR has a winged helix-turn-helix motif that binds to the major groove of the DNA. This structure shows that, in the absence of arginine, the ArgR trimer can bind three ARG box half-sites. It also reveals the structure of the whole MtbArgR molecule itself containing both N-terminal and C-terminal domains. | ||
| - | + | Crystal structure of the arginine repressor protein in complex with the DNA operator from Mycobacterium tuberculosis.,Cherney LT, Cherney MM, Garen CR, Lu GJ, James MN J Mol Biol. 2008 Dec 31;384(5):1330-40. Epub 2008 Oct 15. PMID:18952097<ref>PMID:18952097</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
| + | *[[Arginine repressor|Arginine repressor]] | ||
*[[Tomato aspermy virus protein 2b Suppression of RNA Silencing|Tomato aspermy virus protein 2b Suppression of RNA Silencing]] | *[[Tomato aspermy virus protein 2b Suppression of RNA Silencing|Tomato aspermy virus protein 2b Suppression of RNA Silencing]] | ||
*[[User:Wayne Decatur/Tomato aspermy virus protein 2b Suppression of RNA Silencing|User:Wayne Decatur/Tomato aspermy virus protein 2b Suppression of RNA Silencing]] | *[[User:Wayne Decatur/Tomato aspermy virus protein 2b Suppression of RNA Silencing|User:Wayne Decatur/Tomato aspermy virus protein 2b Suppression of RNA Silencing]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
| - | [[Category: Cherney, L T | + | [[Category: Cherney, L T]] |
| - | [[Category: Cherney, M M | + | [[Category: Cherney, M M]] |
| - | [[Category: Garen, C R | + | [[Category: Garen, C R]] |
| - | [[Category: James, M N | + | [[Category: James, M N]] |
| - | [[Category: Lu, G J | + | [[Category: Lu, G J]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
[[Category: Amino-acid biosynthesis]] | [[Category: Amino-acid biosynthesis]] | ||
[[Category: Arginine biosynthesis]] | [[Category: Arginine biosynthesis]] | ||
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[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] | ||
[[Category: Dna-binding]] | [[Category: Dna-binding]] | ||
| - | [[Category: Mycobacterium tuberculosis]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Tb structural genomic]] | ||
| - | [[Category: Tb structural genomics consortium]] | ||
[[Category: Tbsgc]] | [[Category: Tbsgc]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
Revision as of 14:16, 17 December 2014
Crystal structure of the arginine repressor protein from Mycobacterium tuberculosis in complex with the DNA operator
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Categories: Mycobacterium tuberculosis | Cherney, L T | Cherney, M M | Garen, C R | James, M N | Lu, G J | Structural genomic | Amino-acid biosynthesis | Arginine biosynthesis | Arginine repressor protein | Argr-operator complex | Dna binding | Dna binding protein-dna complex | Dna-binding | Tbsgc | Transcription | Transcription regulation
