5ffc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CopM in the Cu(II)-bound form== | |
| + | <StructureSection load='5ffc' size='340' side='right'caption='[[5ffc]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ffc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FFC 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]] 2.007Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ffc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffc OCA], [https://pdbe.org/5ffc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ffc RCSB], [https://www.ebi.ac.uk/pdbsum/5ffc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6YRW5_SYNY3 Q6YRW5_SYNY3] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Copper homeostasis integrates multiple processes from sensing to storage and efflux out of the cell. CopM is a cyanobacterial metallochaperone, the gene for which is located upstream of a two-component system for copper resistance, but the molecular basis for copper recognition by this four-helical bundle protein is unknown. Here, crystal structures of CopM in apo, copper-bound and silver-bound forms are reported. Monovalent copper/silver ions are buried within the bundle core; divalent copper ions are found on the surface of the bundle. The monovalent copper/silver-binding site is constituted by two consecutive histidines and is conserved in a previously functionally unknown protein family. The structural analyses show two conformational states and suggest that flexibility in the first alpha-helix is related to the metallochaperone function. These results also reveal functional diversity from a protein family with a simple four-helical fold. | ||
| - | + | Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM.,Zhao S, Wang X, Niu G, Dong W, Wang J, Fang Y, Lin Y, Liu L Acta Crystallogr D Struct Biol. 2016 Sep;72(Pt 9):997-1005. doi:, 10.1107/S2059798316011943. Epub 2016 Aug 18. PMID:27599732<ref>PMID:27599732</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ffc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synechocystis sp. PCC 6803]] | ||
| + | [[Category: Liu L]] | ||
| + | [[Category: Wang X]] | ||
| + | [[Category: Zhao S]] | ||
Current revision
CopM in the Cu(II)-bound form
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