1son

ADENYLOSUCCINATE SYNTHETASE IN COMPLEX WITH THE NATURAL FEEDBACK INHIBITOR AMP

spinqualitylabelsall models 1son, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1son is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMP, BME Activity: Adenylosuccinate synthase, with EC number 6.3.4.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PURA_ECOLI] Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[HAMAP-Rule:MF_00011] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed (+)-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. 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.,Fonne-Pfister R, Chemla P, Ward E, Girardet M, Kreuz KE, Honzatko RB, Fromm HJ, Schar HP, Grutter MG, Cowan-Jacob SW Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9431-6. PMID:8790347 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenylosuccinate Synthetase

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