X-RAY STRUCTURE DETERMINATION AT 2.6-ANGSTROM RESOLUTION OF A LIPOATE-CONTAINING PROTEIN - THE H-PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX FROM PEA LEAVES

被引:64
作者
PARES, S
COHENADDAD, C
SIEKER, L
NEUBURGER, M
DOUCE, R
机构
[1] CNRS,INST BIOL STRUCT,F-38027 GRENOBLE,FRANCE
[2] CEA,DEPT CELLULAR & STRUCT BIOL,CNRS,URA 576,F-38054 GRENOBLE 9,FRANCE
[3] CEA,F-38027 GRENOBLE,FRANCE
[4] UNIV WASHINGTON,DEPT BIOL STRUCT,SEATTLE,WA 98195
关键词
D O I
10.1073/pnas.91.11.4850
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
H-protein, a lipoic acid-containing protein of the glycine decarboxylase (EC 1.4.4.2) complex from pea (Pisum sativum) was crystallized from ammonium sulfate solution at pH 5.2 in space group P3(1)21. The x-ray crystal structure was determined to 2.6-Angstrom resolution by multiple isomorphous replacement techniques. The structure was refined to an R value of 23% for reflections between 15- and 2.6-Angstrom, resolution (F > 2 sigma), including the lipoate moiety and 50 water molecules, for the two protein molecules of the asymmetric unit. The 131-amino acid residues form seven beta-strands arranged into two antiparallel beta-sheets forming a ''sandwich'' structure. One alpha-helix is observed at the C-terminal end. The lipoate cofactor attached to Lys-63 is located in the loop of a hairpin configuration. The lipoate moiety points toward the residues His-34 and Asp-128 and is situated at the surface of the H-protein. This allows the flexibility of the lipoate arm. This is the first x-ray determination of a lipoic acid-containing protein, and the present results are in agreement with previous theoretical predictions and NMR studies of the catalytic domains of lipoic acid- and biotin-containing proteins.
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页码:4850 / 4853
页数:4
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