1bl5
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(New page: 200px<br /> <applet load="1bl5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bl5, resolution 2.5Å" /> '''ISOCITRATE DEHYDROGE...)
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Revision as of 19:07, 29 October 2007
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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 [[1]], with EC number [1.1.1.42]. 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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