1LAC
THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX
Summary for 1LAC
| Entry DOI | 10.2210/pdb1lac/pdb |
| Descriptor | DIHYDROLIPOAMIDE ACETYLTRANSFERASE (1 entity in total) |
| Functional Keywords | transferase (acyltransferase) |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 8653.78 |
| Authors | Dardel, F.,Davis, A.L.,Laue, E.D.,Perham, R.N. (deposition date: 1992-09-02, release date: 1993-07-15, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 8445635DOI: 10.1006/jmbi.1993.1103 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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