1bl5

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[[Category: phosphorylation]]
[[Category: phosphorylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:52:23 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:55:46 2007''

Revision as of 12:51, 30 October 2007


1bl5, resolution 2.5Å

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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, ... [(full description)]

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

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