1YAA

ASPARTATE AMINOTRANSFERASE FROM SACCHAROMYCES CEREVISIAE CYTOPLASM

1YAA の概要

• エントリーDOI: 10.2210/pdb1yaa/pdb
• 分子名称: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: transferase, aminotransferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P23542
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 182899.04

構造登録者

Jeffery, C.J. (登録日: 1998-01-27, 公開日: 1998-09-16, 最終更新日: 2023-08-09)

主引用文献

Jeffery, C.J.,Barry, T.,Doonan, S.,Petsko, G.A.,Ringe, D.
Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase.
Protein Sci., 7:1380-1387, 1998

PubMed Abstract: The crystal structure of Saccharomyces cerevisiae cytoplasmic aspartate aminotransferase (EC 2.6.1.1) has been determined to 2.05 A resolution in the presence of the cofactor pyridoxal-5'-phosphate and the competitive inhibitor maleate. The structure was solved by the method of molecular replacement. The final value of the crystallographic R-factor after refinement was 23.1% with good geometry of the final model. The yeast cytoplasmic enzyme is a homodimer with two identical active sites containing residues from each subunit. It is found in the "closed" conformation with a bound maleate inhibitor in each active site. It shares the same three-dimensional fold and active site residues as the aspartate aminotransferases from Escherichia coli, chicken cytoplasm, and chicken mitochondria, although it shares less than 50% sequence identity with any of them. The availability of four similar enzyme structures from distant regions of the evolutionary tree provides a measure of tolerated changes that can arise during millions of years of evolution.

PubMed: 9655342

実験手法

X-RAY DIFFRACTION (2.05 Å)