5FEJ
CopM in the Cu(I)-bound form
Summary for 5FEJ
Entry DOI | 10.2210/pdb5fej/pdb |
Related | 5FFA 5FFB 5FFC 5FFD 5FFE |
Descriptor | CopM, COPPER (I) ION (3 entities in total) |
Functional Keywords | copper-binding protein, metal binding protein |
Biological source | Synechocystis sp. PCC 6803 |
Total number of polymer chains | 4 |
Total formula weight | 82034.30 |
Authors | |
Primary citation | 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, 72:997-1005, 2016 Cited by PubMed Abstract: 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 α-helix is related to the metallochaperone function. These results also reveal functional diversity from a protein family with a simple four-helical fold. PubMed: 27599732DOI: 10.1107/S2059798316011943 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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