5FFB

CopM in the apo form

Summary for 5FFB

• Entry DOI: 10.2210/pdb5ffb/pdb
• Related: 5FEJ 5FFA 5FFC 5FFD 5FFE
• Descriptor: CopM (2 entities in total)
• Functional Keywords: copper binding protein, metal binding protein
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 1
• Total formula weight: 20381.48

Authors

Zhao, S.,Wang, X.,Liu, L. (deposition date: 2015-12-18, release date: 2016-09-07, Last modification date: 2023-11-08)

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

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

Experimental method

X-RAY DIFFRACTION (1.702 Å)