1id2
From Proteopedia
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CRYSTAL STRUCTURE OF AMICYANIN FROM PARACOCCUS VERSUTUS (THIOBACILLUS VERSUTUS)
Overview
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.
About this Structure
1ID2 is a Single protein structure of sequence from Paracoccus versutus with CU as ligand. Full crystallographic information is available from OCA.
Reference
Crystal 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 AP, Canters GW, Durley R, Mathews FS, J Mol Biol. 1994 Mar 4;236(4):1196-211. PMID:8120896
Page seeded by OCA on Tue Nov 20 17:18:00 2007
