The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase
| Autor: | Philippe Chemla, M Girardet, Raymonde Fonne-Pfister, R B Honzatko, E Ward, H J Fromm, K E Kreuz, M G Grütter, Sandra W. Cowan-Jacob, H P Schär |
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| Jazyk: | angličtina |
| Rok vydání: | 1996 |
| Předmět: |
DNA
Complementary Protein Conformation Molecular Sequence Data Crystallography X-Ray Feedback Adenylosuccinate Synthase Protein structure medicine Escherichia coli Amino Acid Sequence Binding site Adenylosuccinate lyase Cells Cultured chemistry.chemical_classification DNA ligase Multidisciplinary Binding Sites biology Sequence Homology Amino Acid Herbicides Hydantoins Adenylosuccinate synthase Plants Adenosine Enzyme Phenotype Biochemistry chemistry biology.protein Phosphorylation medicine.drug Research Article |
| Popis: | (+)-Hydantocidin, a recently discovered natural spironucleoside with potent herbicidal activity, is shown to be a proherbicide that, after phosphorylation at the 5' position, inhibits adenylosuccinate synthetase, an enzyme involved in de novo purine synthesis. The mode of binding of hydantocidin 5'-monophosphate to the target enzyme was analyzed by determining the crystal structure of the enzyme-inhibitor complex at 2.6-A resolution. It was found that adenylosuccinate synthetase binds the phosphorylated compound in the same fashion as it does adenosine 5'-monophosphate, the natural feedback regulator of this enzyme. This work provides the first crystal structure of a herbicide-target complex reported to date. |
| Databáze: | OpenAIRE |
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