Function

Amicyanin (ACY) is a copper protein which is part of a electron transfer complex with Methylamine dehydrogenase and Cytochrome C-551[1]. ACY serves as the electron acceptor for methyl amine dehydrogenase. ACY belongs to type I copper proteins in which the copper is coordinated by 2 His residues, a Lys residue and a variable ligand in a trigonal planar structure.

Structural highlights

The 3D structure of ACY shows that the protein assumes a β-sandwich topology. The Cu+2 binding site has tetragonal geometry with interactions to 2 His, Cys and Met side chains. ACY interacts with methylamine dehydrogenase via a hydrophobic patch and Arg salt bridge[2].

3D structures of amicyanin

Amicyanin 3D structures

Amicyanin complex with Cu+2 (orange), K+ (purple), and phosphate (PDB ID 3ply)

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ReferencesReferences

  1. Zhu Z, Cunane LM, Chen Z, Durley RC, Mathews FS, Davidson VL. Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin. Biochemistry. 1998 Dec 8;37(49):17128-36. PMID:9860825 doi:10.1021/bi9817919
  2. Choi M, Sukumar N, Mathews FS, Liu A, Davidson VL. Proline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein-Protein Interface. Biochemistry. 2011 Jan 26. PMID:21268585 doi:10.1021/bi101794y

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