5jvo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the Arginine Repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis== | |
| + | <StructureSection load='5jvo' size='340' side='right' caption='[[5jvo]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jvo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JVO 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>, <scene name='pdbligand=TYR:TYROSINE'>TYR</scene></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=5jvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jvo OCA], [http://pdbe.org/5jvo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jvo RCSB], [http://www.ebi.ac.uk/pdbsum/5jvo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jvo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A0E3UAP8_CORPS A0A0E3UAP8_CORPS]] Regulates arginine biosynthesis genes.[HAMAP-Rule:MF_00173] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The arginine repressor (ArgR) regulates arginine biosynthesis in a number of microorganisms and consists of two domains interlinked by a short peptide; the N-terminal domain is involved in DNA binding and the C-terminal domain binds arginine and forms a hexamer made-up of a dimer of trimers. The crystal structure of the C-terminal domain of ArgR from the pathogenic Corynebacterium pseudotuberculosis determined at 1.9 A resolution contains a tightly bound tyrosine at the arginine-binding site indicating hitherto unobserved promiscuity. Structural analysis of the binding pocket displays clear molecular adaptations to accommodate tyrosine binding suggesting the possible existence of an alternative regulatory process in this pathogenic bacterium. | ||
| - | + | Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis.,Mariutti RB, Ullah A, Araujo GC, Murakami MT, Arni RK Biochem Biophys Res Commun. 2016 Jul 8;475(4):350-5. doi:, 10.1016/j.bbrc.2016.05.091. Epub 2016 May 24. PMID:27233609<ref>PMID:27233609</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Arni, R | + | <div class="pdbe-citations 5jvo" style="background-color:#fffaf0;"></div> |
| - | [[Category: Mariutti, R | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arni, R K]] | ||
| + | [[Category: Mariutti, R B]] | ||
| + | [[Category: Murakami, M T]] | ||
[[Category: Ullah, A]] | [[Category: Ullah, A]] | ||
| - | [[Category: | + | [[Category: Arginine repressor]] |
| + | [[Category: Dna binding protein]] | ||
Revision as of 13:56, 10 September 2016
Crystal structure of the Arginine Repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis
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