1BL5

ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION

1BL5 の概要

• エントリーDOI: 10.2210/pdb1bl5/pdb
• 分子名称: ISOCITRATE DEHYDROGENASE, MAGNESIUM ION, 2-OXOGLUTARIC ACID, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, nad(a)-choh(d), phosphorylation
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46463.07

構造登録者

Stoddard, B.L.,Cohen, B.,Brubaker, M.,Mesecar, A.,Koshland Junior, D.E. (登録日: 1998-07-23, 公開日: 1999-05-04, 最終更新日: 2024-02-07)

主引用文献

Stoddard, B.L.,Cohen, B.E.,Brubaker, M.,Mesecar, A.D.,Koshland Jr., D.E.
Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs.
Nat.Struct.Biol., 5:891-897, 1998

PubMed Abstract: The structure of a rate-limited product complex formed during a single initial round of turnover by isocitrate dehydrogenase has been determined. Photolytic liberation of either caged substrate or caged cofactor and Laue X-ray data collection were used to visualize the complex, which has a minimum half-life of approximately 10 milliseconds. The experiment was conducted with three different photoreactive compounds, each possessing a unique mechanism leading to the formation of the enzyme-substrate (ES) complex. Photoreaction efficiency and subsequent substrate affinities and binding rates in the crystal are critical parameters for these experiments. The structure suggests that CO2 dissociation is a rapid event that may help drive product formation, and that small conformational changes may contribute to slow product release.

PubMed: 9783749
DOI: 10.1038/2331

実験手法

X-RAY DIFFRACTION (2.5 Å)