1bl5
From Proteopedia
ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION
Overview
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.
About this Structure
1BL5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs., Stoddard BL, Cohen BE, Brubaker M, Mesecar AD, Koshland DE Jr, Nat Struct Biol. 1998 Oct;5(10):891-7. PMID:9783749 Page seeded by OCA on Fri May 2 11:39:18 2008
