1lab
THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
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Overview
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.
About this Structure
1LAB is a Single protein structure of sequence from Geobacillus stearothermophilus. Active as Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex., Dardel F, Davis AL, Laue ED, Perham RN, J Mol Biol. 1993 Feb 20;229(4):1037-48. PMID:8445635
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