Three-Dimensional Structure of Aspartate Aminotransferase from Escherichia coli at 2.8 Å Resolution

Shigehiro Kamitori; Ken Hirotsu; Taiichi Higuchi; Kiyoshi Kondo; Katsura Inoue; Seiki Kuramitsu; Hiroyuki Kagamiyama; Yoshiki Higuchi; Noritake Yasuoka; Masami Kusunoki; Yoshiki Matsuura

Shigehiro Kamitori, Ken Hirotsu, Taiichi Higuchi, Kiyoshi Kondo, Katsura Inoue, Seiki Kuramitsu, Hiroyuki Kagamiyama, Yoshiki Higuchi, Noritake Yasuoka, Masami Kusunoki, Yoshiki Matsuura

Author information

Shigehiro Kamitori
Department of Chemistry, Faculty of Science, Osaka City University
Ken Hirotsu
Department of Chemistry, Faculty of Science, Osaka City University
Taiichi Higuchi
Department of Chemistry, Faculty of Science, Osaka City University
Kiyoshi Kondo
Department of Medical Chemistry, Osaka Medical College
Katsura Inoue
Department of Medical Chemistry, Osaka Medical College
Seiki Kuramitsu
Department of Medical Chemistry, Osaka Medical College
Hiroyuki Kagamiyama
Department of Medical Chemistry, Osaka Medical College
Yoshiki Higuchi
Basic Research Laboratory, Himeji Institute of Technology
Noritake Yasuoka
Basic Research Laboratory, Himeji Institute of Technology
Masami Kusunoki
Institute for Protein Research, Osaka University
Yoshiki Matsuura
Institute for Protein Research, Osaka University

JOURNAL FREE ACCESS

1988 Volume 104 Issue 3 Pages 317-318

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Abstract

The crystal structure of aspartate aminotransferase of Escherichia coli was determined by X-ray structure analysis at 2.8 Å resolution. The structure was solved by the molecular replacement method and refined to an R-factor of 0.27, and it was found that the overall structure of AspAT of E. coli is similar to that of those of higher animals.

Corresponding author

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