1SOO

ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE

Summary for 1SOO

• Entry DOI: 10.2210/pdb1soo/pdb
• Descriptor: ADENYLOSUCCINATE SYNTHETASE, SULFATE ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: purine nucleotide biosynthesis, gtp-hydrolyzing enzyme, herbicide, ligase, synthetase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7D4
• Total number of polymer chains: 1
• Total formula weight: 47957.05

Authors

Cowan-Jacob, S.W. (deposition date: 1996-05-07, release date: 1997-09-04, Last modification date: 2023-08-09)

Primary citation

Fonne-Pfister, R.,Chemla, P.,Ward, E.,Girardet, M.,Kreuz, K.E.,Honzatko, R.B.,Fromm, H.J.,Schar, H.P.,Grutter, M.G.,Cowan-Jacob, S.W.
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.
Proc.Natl.Acad.Sci.USA, 93:9431-9436, 1996

PubMed 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.

PubMed: 8790347
DOI: 10.1073/pnas.93.18.9431

Experimental method

X-RAY DIFFRACTION (2.6 Å)