CRYSTAL-STRUCTURE ANALYSIS AND REFINEMENT AT 2-CENTER-DOT-15 ANGSTROM RESOLUTION OF AMICYANIN, A TYPE-I BLUE COPPER PROTEIN, FROM THIOBACILLUS-VERSUTUS

被引:78
作者
ROMERO, A
NAR, H
HUBER, R
MESSERSCHMIDT, A
KALVERDA, AP
CANTERS, GW
DURLEY, R
MATHEWS, FS
机构
[1] MAX PLANCK INST BIOCHEM,STRUKT FORSCH ABT,W-8033 MARTINSRIED,GERMANY
[2] LEIDEN UNIV,GORLAEUS LABS,DEPT CHEM,2300 RA LEIDEN,NETHERLANDS
[3] WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOLEC BIOPHYS,ST LOUIS,MO 63110
关键词
AMICYANIN; PROTEIN CRYSTALLOGRAPHY; TYPE I BLUE COPPER PROTEIN; ELECTRON TRANSFER; 3-DIMENSIONAL STRUCTURE;
D O I
10.1016/0022-2836(94)90021-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 P32 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 32 axes. The final R-value is 17·4% for 15,984 reflections to a resolution of 2·15 Å. The polypeptide fold in amicyanin is based on the β-sandwich structure commonly found in blue copper proteins. Nine β strands are folded into two twisted β-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. © 1994.
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页码:1196 / 1211
页数:16
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