5ffd | pdb_00005ffd

CopM in the Ag-bound form (by co-crystallization)

spinqualitylabelsall models 5ffd, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ffd is a 1 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.451Å Ligands: AG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6YRW5_SYNY3 Publication Abstract from PubMed 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 alpha-helix is related to the metallochaperone function. These results also reveal functional diversity from a protein family with a simple four-helical fold. Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM.,Zhao S, Wang X, Niu G, Dong W, Wang J, Fang Y, Lin Y, Liu L Acta Crystallogr D Struct Biol. 2016 Sep;72(Pt 9):997-1005. doi:, 10.1107/S2059798316011943. Epub 2016 Aug 18. PMID:27599732 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA