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

doi:10.1021/bi00446a030

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 journal › Article › peer-review

107 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 language	English (US)
Pages (from-to)	8161-8167
Number of pages	7
Journal	Biochemistry
Volume	28
Issue number	20
DOIs	https://doi.org/10.1021/bi00446a030
State	Published - 1989
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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title = "2.8-{\AA}-Resolution Crystal Structure of an Active-Site Mutant of Aspartate Aminotransferase from Escherichia coli",

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-{\AA} 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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year = "1989",

doi = "10.1021/bi00446a030",

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pages = "8161--8167",

journal = "Biochemistry",

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T1 - 2.8-Å-Resolution Crystal Structure of an Active-Site Mutant of Aspartate Aminotransferase from Escherichia coli

AU - Smith, Douglas L.

AU - Almo, Steven C.

AU - Toney, Michael D.

AU - Ringe, Dagmar

PY - 1989

Y1 - 1989

N2 - 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.

AB - 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.

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JO - Biochemistry

JF - Biochemistry

IS - 20

ER -

2.8-Å-Resolution Crystal Structure of an Active-Site Mutant of Aspartate Aminotransferase from Escherichia coli

Abstract

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