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PDBsum entry 5ffe
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Metal binding protein
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PDB id
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5ffe
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References listed in PDB file
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Key reference
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Title
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Structural basis for copper/silver binding by the synechocystis metallochaperone copm.
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Authors
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S.Zhao,
X.Wang,
G.Niu,
W.Dong,
J.Wang,
Y.Fang,
Y.Lin,
L.Liu.
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Ref.
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Acta Crystallogr D Struct Biol, 2016,
72,
997.
[DOI no: ]
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PubMed id
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Abstract
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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.
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