Download MendeleyCrystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus.
Romero, A., Nar, H., Huber, R., Messerschmidt, A., Kalverda, A.P., Canters, G.W., Durley, R., Mathews, F.S.(1994) J Mol Biol 236: 1196-1211
- PubMed: 8120896
- DOI: https://doi.org/10.1016/0022-2836(94)90021-3
- Primary Citation of Related Structures:
1ID2 - PubMed Abstract:
The crystal structure of the type I blue copper protein amicyanin from Thiobacillus versutus has been determined by Patterson search techniques on the basis of the molecular model of amicyanin from Paracoccus denitrificans, and refined by energy-restrained least-squares methods. Amicyanin crystallizes in the trigonal space group P3(2) with unit cell dimensions of a = b = 87.40 A, c = 38.20 A. The asymmetric unit is composed of three independent molecules centred on the crystallographic 3(2) axes. The final R-value is 17.4% for 15,984 reflections to a resolution of 2.15 A. The polypeptide fold in amicyanin is based on the beta-sandwich structure commonly found in blue copper proteins. Nine beta strands are folded into two twisted beta-sheets that pack together with a filling of non-polar residues between them. The geometry of the copper site is similar to that of plastocyanin. There are four ligands, arranged approximately as a distorted tetrahedron, to the copper atom: His54, Cys93, His96 and Met99. One of the copper ligands, His96, is exposed to the surface and lies in the centre of a cluster of seven hydrophobic residues.
Organizational Affiliation:
Max-Planck Institut für Biochemie, Abteilung Strukturforschung, Martinsried bei München, Germany.
