1YPI

STRUCTURE OF YEAST TRIOSEPHOSPHATE ISOMERASE AT 1.9-ANGSTROMS RESOLUTION

1YPI の概要

• エントリーDOI: 10.2210/pdb1ypi/pdb
• 分子名称: TRIOSEPHOSPHATE ISOMERASE (2 entities in total)
• 機能のキーワード: isomerase(intramolecular oxidoreductase)
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53392.45

構造登録者

Alber, T.,Lolis, E.,Petsko, G.A. (登録日: 1990-01-12, 公開日: 1991-01-15, 最終更新日: 2024-02-14)

主引用文献

Lolis, E.,Alber, T.,Davenport, R.C.,Rose, D.,Hartman, F.C.,Petsko, G.A.
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Biochemistry, 29:6609-6618, 1990

PubMed Abstract: The structure of yeast triosephosphate isomerase (TIM) has been solved at 3.0-A resolution and refined at 1.9-A resolution to an R factor of 21.0%. The final model consists of all non-hydrogen atoms in the polypeptide chain and 119 water molecules, a number of which are found in the interior of the protein. The structure of the active site clearly indicates that the carboxylate of the catalytic base, Glu 165, is involved in a hydrogen-bonding interaction with the hydroxyl of Ser 96. In addition, the interactions of the other active site residues, Lys 12 and His 95, are also discussed. For the first time in any TIM structure, the "flexible loop" has well-defined density; the conformation of the loop in this structure is stabilized by a crystal contact. Analysis of the subunit interface of this dimeric enzyme hints at the source of the specificity of one subunit for another and allows us to estimate an association constant of 10(14)-10(16) M-1 for the two monomers. The analysis also suggests that the interface may be a particularly good target for drug design. The conserved positions (20%) among sequences from 13 sources ranging on the evolutionary scale from Escherichia coli to humans reveal the intense pressure to maintain the active site structure.

PubMed: 2204417
DOI: 10.1021/bi00480a009

実験手法

X-RAY DIFFRACTION (1.9 Å)