1LAC

THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX

1LAC の概要

• エントリーDOI: 10.2210/pdb1lac/pdb
• 分子名称: DIHYDROLIPOAMIDE ACETYLTRANSFERASE (1 entity in total)
• 機能のキーワード: transferase (acyltransferase)
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8653.78

構造登録者

Dardel, F.,Davis, A.L.,Laue, E.D.,Perham, R.N. (登録日: 1992-09-02, 公開日: 1993-07-15, 最終更新日: 2024-05-01)

主引用文献

Dardel, F.,Davis, A.L.,Laue, E.D.,Perham, R.N.
Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
J.Mol.Biol., 229:1037-1048, 1993

PubMed Abstract: The structure of the lipoyl domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus has been determined by means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear Overhauser effect distance constraints and 76 dihedral angle restraints were employed as the input for the structure calculations, which were performed using a hybrid distance geometry-simulated annealing strategy and the programs DISGEO and X-PLOR. The overall structure of the lipoyl domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase polypeptide chain) is that of a flattened eight-stranded beta-barrel folded around a core of well-defined hydrophobic residues. The lipoylation site, lysine 42, is located in the middle of a beta-turn, and the N and C-terminal residues of the domain are close together in adjacent beta-strands at the opposite end of the molecule. The polypeptide backbone exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of residues 15 to 39 and 52 to 76 being almost superimposable on those of residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation = 1.48 A). The amino acid residues at key positions in the structure are conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.

PubMed: 8445635
DOI: 10.1006/jmbi.1993.1103

実験手法

SOLUTION NMR