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PDBsum entry 1lab
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Transferase (acyltransferase)
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PDB id
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1lab
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References listed in PDB file
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Key reference
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Title
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Three-Dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
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Authors
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F.Dardel,
A.L.Davis,
E.D.Laue,
R.N.Perham.
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Ref.
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J Mol Biol, 1993,
229,
1037-1048.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Sequence-Specific 1h-Nmr assignments and secondary structure of the lipoyl domain of the bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
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Authors
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F.Dardel,
E.D.Laue,
R.N.Perham.
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Ref.
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Eur J Biochem, 1991,
201,
203-209.
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PubMed id
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