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| | <StructureSection load='5ffb' size='340' side='right'caption='[[5ffb]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5ffb' size='340' side='right'caption='[[5ffb]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ffb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FFB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ffb]] is a 1 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=5FFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FFB FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fej|5fej]], [[5ffa|5ffa]], [[5ffc|5ffc]], [[5ffd|5ffd]], [[5ffe|5ffe]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.702Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcopM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</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=5ffb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffb OCA], [https://pdbe.org/5ffb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ffb RCSB], [https://www.ebi.ac.uk/pdbsum/5ffb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffb ProSAT]</span></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=5ffb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffb OCA], [http://pdbe.org/5ffb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ffb RCSB], [http://www.ebi.ac.uk/pdbsum/5ffb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6YRW5_SYNY3 Q6YRW5_SYNY3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, L]] | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Wang, X]] | + | [[Category: Liu L]] |
| - | [[Category: Zhao, S]] | + | [[Category: Wang X]] |
| - | [[Category: Copper binding protein]] | + | [[Category: Zhao S]] |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
Q6YRW5_SYNY3
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao S, Wang X, Niu G, Dong W, Wang J, Fang Y, Lin Y, Liu L. Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM. Acta Crystallogr D Struct Biol. 2016 Sep;72(Pt 9):997-1005. doi:, 10.1107/S2059798316011943. Epub 2016 Aug 18. PMID:27599732 doi:http://dx.doi.org/10.1107/S2059798316011943
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