1ID2

CRYSTAL STRUCTURE OF AMICYANIN FROM PARACOCCUS VERSUTUS (THIOBACILLUS VERSUTUS)

Summary for 1ID2

• Entry DOI: 10.2210/pdb1id2/pdb
• Related: 1AAC 1AAJ 1AAN 1BXA 1MDA 2RAC
• Descriptor: AMICYANIN, COPPER (II) ION (3 entities in total)
• Functional Keywords: beta barrel, type-1 blue copper protein, electron transfer protein, electron transport
• Biological source: Paracoccus versutus
• Cellular location: Periplasm: P22365
• Total number of polymer chains: 3
• Total formula weight: 35300.79

Authors

Romero, A.,Nar, H.,Messerschmidt, A. (deposition date: 2001-04-03, release date: 2001-04-11, Last modification date: 2024-02-07)

Primary citation

Romero, A.,Nar, H.,Huber, R.,Messerschmidt, A.,Kalverda, A.P.,Canters, G.W.,Durley, R.,Mathews, F.S.
Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus.
J.Mol.Biol., 236:1196-1211, 1994

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.

PubMed: 8120896
DOI: 10.1016/0022-2836(94)90021-3

Experimental method

X-RAY DIFFRACTION (2.15 Å)