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. 1996 Sep 3;93(18):9431–9436. doi: 10.1073/pnas.93.18.9431

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.

R Fonné-Pfister 1, P Chemla 1, E Ward 1, M Girardet 1, K E Kreuz 1, R B Honzatko 1, H J Fromm 1, H P Schär 1, M G Grütter 1, S W Cowan-Jacob 1
PMCID: PMC38445  PMID: 8790347

Abstract

(+)-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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