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PDBsum entry 1soo

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Ligase PDB id
1soo
Contents
Protein chain
431 a.a.
Ligands
SO4 ×3
H5P
BME
Metals
_NA
Waters ×78

References listed in PDB file
Key reference
Title 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.
Authors R.Fonné-Pfister, P.Chemla, E.Ward, M.Girardet, K.E.Kreuz, R.B.Honzatko, H.J.Fromm, H.P.Schär, M.G.Grütter, S.W.Cowan-Jacob.
Ref. Proc Natl Acad Sci U S A, 1996, 93, 9431-9436.
PubMed id 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.
Secondary reference #1
Title Refined crystal structures of unligated adenylosuccinate synthetase from escherichia coli.
Authors M.M.Silva, B.W.Poland, C.R.Hoffman, H.J.Fromm, R.B.Honzatko.
Ref. J Mol Biol, 1995, 254, 431-446. [DOI no: 10.1006/jmbi.1995.0629]
PubMed id 7490761
Full text Abstract
Figure 1.
Figure 1. Amino acid sequence used in the refinement of unligated crystal structures of the synthetase.
Figure 8.
Figure 8. Identification of the active site of the synthetase (top) by the location of IMP and GDP in a preliminary crystal structure, (middle) by directed mutation, and (bottom) by the mapping of conserved residues of synthetases from bacteria, yeast and mammals. Drawing by MOLSCRIPT (Kraulis, 1991).
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #2
Title Crystal structure of adenylosuccinate synthetase from escherichia coli. Evidence for convergent evolution of gtp-Binding domains.
Authors B.W.Poland, M.M.Silva, M.A.Serra, Y.Cho, K.H.Kim, E.M.Harris, R.B.Honzatko.
Ref. J Biol Chem, 1993, 268, 25334-25342.
PubMed id 8244965
Abstract
Secondary reference #3
Title Preliminary X-Ray crystallographic study of adenylosuccinate synthetase from escherichia coli.
Authors M.A.Serra, M.B.Bass, H.J.Fromm, R.B.Honzatko.
Ref. J Mol Biol, 1988, 200, 753-754.
PubMed id 3045328
Abstract
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