1bl5

From Proteopedia

Revision as of 13:50, 5 November 2007

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 with MG, AKG and NAP as ligands. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Structure known Active Site: SUB. 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 Mon Nov 5 15:55:30 2007