5ffc
From Proteopedia
(Difference between revisions)
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==CopM in the Cu(II)-bound form== | ==CopM in the Cu(II)-bound form== | ||
| - | <StructureSection load='5ffc' size='340' side='right' caption='[[5ffc]], [[Resolution|resolution]] 2.01Å' scene=''> | + | <StructureSection load='5ffc' size='340' side='right'caption='[[5ffc]], [[Resolution|resolution]] 2.01Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5ffc]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FFC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ffc]] is a 2 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=5FFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FFC FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <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">[[5fej|5fej]], [[5ffa|5ffa]], [[5ffb|5ffb]], [[5ffd|5ffd]], [[5ffe|5ffe]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fej|5fej]], [[5ffa|5ffa]], [[5ffb|5ffb]], [[5ffd|5ffd]], [[5ffe|5ffe]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ffc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffc OCA], [http://pdbe.org/5ffc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ffc RCSB], [http://www.ebi.ac.uk/pdbsum/5ffc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffc 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=5ffc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffc OCA], [http://pdbe.org/5ffc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ffc RCSB], [http://www.ebi.ac.uk/pdbsum/5ffc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5ffc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Liu, L]] | [[Category: Liu, L]] | ||
[[Category: Wang, X]] | [[Category: Wang, X]] | ||
Revision as of 11:38, 25 December 2019
CopM in the Cu(II)-bound form
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