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

Research output: Contribution to journalArticle

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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

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Aspartate Aminotransferases
Escherichia coli
Lysine
Catalytic Domain
Mitochondrial Aspartate Aminotransferase
Crystal structure
Pyridoxamine
Tryptophan
X-Ray Diffraction
Alanine
X ray diffraction
Enzymes
pyridoxamine phosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

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.

2.8-Å-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. / Smith, Douglas L.; Almo, Steven C.; Toney, Michael D.; Ringe, Dagmar.

In: Biochemistry, Vol. 28, No. 20, 1989, p. 8161-8167.

Research output: Contribution to journalArticle

Smith, DL, Almo, SC, Toney, MD & Ringe, D 1989, '2.8-Å-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli', Biochemistry, vol. 28, no. 20, pp. 8161-8167.
Smith, Douglas L. ; Almo, Steven C. ; Toney, Michael D. ; Ringe, Dagmar. / 2.8-Å-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. In: Biochemistry. 1989 ; Vol. 28, No. 20. pp. 8161-8167.
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