1BL5
ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION
Summary for 1BL5
| Entry DOI | 10.2210/pdb1bl5/pdb |
| Descriptor | ISOCITRATE DEHYDROGENASE, MAGNESIUM ION, 2-OXOGLUTARIC ACID, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, nad(a)-choh(d), phosphorylation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 46463.07 |
| Authors | Stoddard, B.L.,Cohen, B.,Brubaker, M.,Mesecar, A.,Koshland Junior, D.E. (deposition date: 1998-07-23, release date: 1999-05-04, Last modification date: 2024-02-07) |
| Primary citation | Stoddard, B.L.,Cohen, B.E.,Brubaker, M.,Mesecar, A.D.,Koshland Jr., D.E. Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs. Nat.Struct.Biol., 5:891-897, 1998 Cited by PubMed Abstract: 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. PubMed: 9783749DOI: 10.1038/2331 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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