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Title
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2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
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Authors
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D.L.Smith,
S.C.Almo,
M.D.Toney,
D.Ringe.
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Ref.
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Biochemistry, 1989,
28,
8161-8167.
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PubMed id
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Abstract
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The three-dimensional structure of a mutant of the aspartate aminotransferase
from Escherichia coli, in which the active-site lysine has been substituted by
alanine (K258A), has been determined at 2.8-A resolution by X-ray diffraction.
The mutant enzyme contains pyridoxamine phosphate as cofactor. The structure is
compared to that of the mitochondrial aspartate aminotransferase. The most
striking differences, aside from the absence of the lysine side chain, occur in
the positions of the pyridoxamine group and of tryptophan 140.
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