title: Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus.
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.
authors.affiliation: Max-Planck Institut für Biochemie, Abteilung Strukturforschung, Martinsried bei München, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Romero
authors.forename: H
authors.initials: H
authors.lastname: Nar
authors.forename: R
authors.initials: R
authors.lastname: Huber
authors.forename: A
authors.initials: A
authors.lastname: Messerschmidt
authors.forename: A P
authors.initials: AP
authors.lastname: Kalverda
authors.forename: G W
authors.initials: GW
authors.lastname: Canters
authors.forename: R
authors.initials: R
authors.lastname: Durley
authors.forename: F S
authors.initials: FS
authors.lastname: Mathews
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D003300:Copper / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D004579:Electron Transport; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry; D010231:Paracoccus denitrificans / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013855:Thiobacillus / Q000737:chemistry* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; C017079:mauC protein, Methylobacterium extorquens; D003300:Copper; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors