1lab
From Proteopedia
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THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
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
Page seeded by OCA on Tue Nov 20 20:25:23 2007
