3k7r
From Proteopedia
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| - | {{STRUCTURE_3k7r| PDB=3k7r | SCENE= }} | ||
| - | ===Crystal structure of [TM][CuAtx1]3=== | ||
| - | {{ABSTRACT_PUBMED_19965379}} | ||
| - | == | + | ==Crystal structure of [TM][CuAtx1]3== |
| - | [[http://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST | + | <StructureSection load='3k7r' size='340' side='right'caption='[[3k7r]], [[Resolution|resolution]] 2.28Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3k7r]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K7R FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4SM:TETRATHIOMOLYBDATE'>4SM</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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=3k7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7r OCA], [https://pdbe.org/3k7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k7r RCSB], [https://www.ebi.ac.uk/pdbsum/3k7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k7r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity. | ||
| + | == 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/k7/3k7r_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/main_output.php?pdb_ID=3k7r ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tetrathiomolybdate (TM) is an orally active agent for treatment of disorders of copper metabolism. Here we describe how TM inhibits proteins that regulate copper physiology. Crystallographic results reveal that the surprising stability of the drug complex with the metallochaperone Atx1 arises from formation of a sulfur-bridged copper-molybdenum cluster reminiscent of those found in molybdenum and iron sulfur proteins. Spectroscopic studies indicate that this cluster is stable in solution and corresponds to physiological clusters isolated from TM-treated Wilson's disease animal models. Finally, mechanistic studies show that the drug-metallochaperone inhibits metal transfer functions between copper-trafficking proteins. The results are consistent with a model wherein TM can directly and reversibly down-regulate copper delivery to secreted metalloenzymes and suggest that proteins involved in metal regulation might be fruitful drug targets. | ||
| - | + | Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation.,Alvarez HM, Xue Y, Robinson CD, Canalizo-Hernandez MA, Marvin RG, Kelly RA, Mondragon A, Penner-Hahn JE, O'Halloran TV Science. 2010 Jan 15;327(5963):331-4. Epub 2009 Nov 26. PMID:19965379<ref>PMID:19965379</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 3k7r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Alvarez | + | [[Category: Alvarez HM]] |
| - | [[Category: | + | [[Category: Mondragon A]] |
| - | [[Category: | + | [[Category: O'Halloran TV]] |
| - | [[Category: Robinson | + | [[Category: Robinson CD]] |
| - | [[Category: Xue | + | [[Category: Xue Y]] |
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Current revision
Crystal structure of [TM][CuAtx1]3
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