1bl5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of a rate-limited product complex formed during a single | + | 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== | ==About this Structure== | ||
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[[Category: Brubaker, M.]] | [[Category: Brubaker, M.]] | ||
[[Category: Cohen, B.]] | [[Category: Cohen, B.]] | ||
| - | [[Category: Junior, D | + | [[Category: Junior, D E.Koshland.]] |
[[Category: Mesecar, A.]] | [[Category: Mesecar, A.]] | ||
| - | [[Category: Stoddard, B | + | [[Category: Stoddard, B L.]] |
[[Category: AKG]] | [[Category: AKG]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:27 2008'' |
Revision as of 09:56, 21 February 2008
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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 changes may contribute to slow product release.
About this Structure
1BL5 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Known structural/functional Site: . 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 Thu Feb 21 11:56:27 2008
