This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5ffa
From Proteopedia
(Difference between revisions)
m (Protected "5ffa" [edit=sysop:move=sysop]) |
|||
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==CopM (with an N-terminal His-tag) in the apo form== | |
| + | <StructureSection load='5ffa' size='340' side='right'caption='[[5ffa]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ffa]] 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=5FFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FFA 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]] 1.501Å</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=5ffa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffa OCA], [https://pdbe.org/5ffa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ffa RCSB], [https://www.ebi.ac.uk/pdbsum/5ffa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffa 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> |
| - | [[Category: | + | <div class="pdbe-citations 5ffa" 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 (with an N-terminal His-tag) in the apo form
| |||||||||||
