1soo

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[[Image:1soo.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1soo| PDB=1soo | SCENE= }}
{{STRUCTURE_1soo| PDB=1soo | SCENE= }}
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'''ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE'''
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===ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE===
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==Overview==
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(+)-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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(as it appears on PubMed at http://www.pubmed.gov), where 8790347 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8790347}}
==About this Structure==
==About this Structure==
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[[Category: Purine nucleotide biosynthesis]]
[[Category: Purine nucleotide biosynthesis]]
[[Category: Synthetase]]
[[Category: Synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:57:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:37:11 2008''

Revision as of 22:37, 28 July 2008

Image:1soo.png

Template:STRUCTURE 1soo

ADENYLOSUCCINATE SYNTHETASE INHIBITED BY HYDANTOCIDIN 5'-MONOPHOSPHATE

Template:ABSTRACT PUBMED 8790347

About this Structure

1SOO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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