1C9C

ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE

1C9C の概要

• エントリーDOI: 10.2210/pdb1c9c/pdb
• 関連するPDBエントリー: 1CQ6 1CQ7 1CQ8
• 分子名称: ASPARTATE AMINOTRANSFERASE, ALANYL-PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: enzyme-substrate complex, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P00509
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43939.45

構造登録者

Ishijima, J.,Nakai, T.,Kawaguchi, S.,Hirotsu, K.,Kuramitsu, S. (登録日: 1999-08-02, 公開日: 2000-12-20, 最終更新日: 2024-02-07)

主引用文献

Ishijima, J.,Nakai, T.,Kawaguchi, S.,Hirotsu, K.,Kuramitsu, S.
Free energy requirement for domain movement of an enzyme
J.Biol.Chem., 275:18939-18945, 2000

PubMed Abstract: Domain movement is sometimes essential for substrate recognition by an enzyme. X-ray crystallography of aminotransferase with a series of aliphatic substrates showed that the domain movement of aspartate aminotransferase was changed dramatically from an open to a closed form by the addition of only one CH(2) to the side chain of the C4 substrate CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63; Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364) enabled us to estimate the free energy required for the domain movement.

PubMed: 10858450
DOI: 10.1074/jbc.275.25.18939

実験手法

X-RAY DIFFRACTION (2.4 Å)