PDBsum entry 5ffa

Metal binding protein

PDB id

5ffa

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Contents

			Protein chain

					135 a.a.

			Waters ×229

PDB id:

5ffa

Links

Name:

Metal binding protein

Title:

Copm (with an n-terminal his-tag) in the apo form

Structure:

Copm. Chain: a. Engineered: yes

Source:

Synechocystis sp. Pcc 6803. Organism_taxid: 1148. Gene: pcopm. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.50Å

R-factor:

0.191

R-free:

0.218

Authors:

S.Zhao,X.Wang,L.Liu

Key ref:

S.Zhao et al. (2016). Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM. Acta Crystallogr D Struct Biol, 72, 997. PubMed id: 27599732 DOI: 10.1107/S2059798316011943

Date:

18-Dec-15

Release date:

07-Sep-16

PROCHECK

	Headers

	References

Protein chain

Q6YRW5 (Q6YRW5_SYNY3) - Slr6039 protein from Synechocystis sp. (strain PCC 6803 / Kazusa)

Seq: Struc:					196 a.a. 135 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1107/S2059798316011943	Acta Crystallogr D Struct Biol 72:997 (2016)
PubMed id: 27599732

Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM.
S.Zhao, X.Wang, G.Niu, W.Dong, J.Wang, Y.Fang, Y.Lin, L.Liu.

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.