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5FEJ

CopM in the Cu(I)-bound form

Summary for 5FEJ
Entry DOI10.2210/pdb5fej/pdb
Related5FFA 5FFB 5FFC 5FFD 5FFE
DescriptorCopM, COPPER (I) ION (3 entities in total)
Functional Keywordscopper-binding protein, metal binding protein
Biological sourceSynechocystis sp. PCC 6803
Total number of polymer chains4
Total formula weight82034.30
Authors
Zhao, S.,Wang, X.,Liu, L. (deposition date: 2015-12-17, release date: 2016-09-07, Last modification date: 2023-11-08)
Primary citationZhao, 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: 27599732
DOI: 10.1107/S2059798316011943
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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数据于2025-07-23公开中

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