2.8-Å-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli

Douglas L. Smith, Steven C. Almo, Michael D. Toney, Dagmar Ringe

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101 Scopus citations

Abstract

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-Å 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.

Original languageEnglish (US)
Pages (from-to)8161-8167
Number of pages7
JournalBiochemistry
Volume28
Issue number20
StatePublished - 1989

ASJC Scopus subject areas

  • Biochemistry

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    Smith, D. L., Almo, S. C., Toney, M. D., & Ringe, D. (1989). 2.8-Å-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. Biochemistry, 28(20), 8161-8167.