2AAT

2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI

2AAT の概要

• エントリーDOI: 10.2210/pdb2aat/pdb
• 分子名称: ASPARTATE AMINOTRANSFERASE, SULFATE ION, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: transferase(aminotransferase)
• 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: 43905.35

構造登録者

Smith, D.,Almo, S.C.,Toney, M.,Ringe, D. (登録日: 1989-05-30, 公開日: 1989-10-15, 最終更新日: 2024-02-14)

主引用文献

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

PubMed 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-A 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.

PubMed: 2513875
DOI: 10.1021/bi00446a030

実験手法

X-RAY DIFFRACTION (2.8 Å)