PDBsum entry 1soo

Ligase

PDB id

1soo

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Contents

			Protein chain

					431 a.a. *

			Ligands

					SO4 ×3


					H5P


					BME

			Metals

					_NA

			Waters ×78

* Residue conservation analysis

PDB id:

1soo

Links

Name:

Ligase

Title:

Adenylosuccinate synthetase inhibited by hydantocidin 5'-monophosphate

Structure:

Adenylosuccinate synthetase. Chain: a. Ec: 6.3.4.4

Source:

Escherichia coli. Organism_taxid: 562. Strain: pur a strain h1238

Biol. unit:

Dimer (from PDB file)

Resolution:

2.60Å

R-factor:

0.187

Authors:

S.W.Cowan-Jacob

Key ref:

R.Fonné-Pfister et al. (1996). 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 U S A, 93, 9431-9436. PubMed id: 8790347

Date:

07-May-96

Release date:

04-Sep-97

PROCHECK

	Headers

	References

Protein chain

P0A7D4 (PURA_ECOLI) - Adenylosuccinate synthetase from Escherichia coli (strain K12)

Seq: Struc:					432 a.a. 431 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.6.3.4.4 - adenylosuccinate synthase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

AMP and GMP Biosynthesis

Reaction:

IMP + L-aspartate + GTP = N₆-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H⁺

IMP

L-aspartate
Bound ligand (Het Group name = H5P)
matches with 68.00% similarity

GTP

N(6)-(1,2-dicarboxyethyl)-AMP

GDP

phosphate

2 × H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	Proc Natl Acad Sci U S A 93:9431-9436 (1996)
PubMed id: 8790347

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, 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.

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

17942678

S.O.Duke (2007).
The emergence of grass root chemical ecology.

Proc Natl Acad Sci U S A, 104, 16729-16730.

16669783

R.Zrenner, M.Stitt, U.Sonnewald, and R.Boldt (2006).
Pyrimidine and purine biosynthesis and degradation in plants.

Annu Rev Plant Biol, 57, 805-836.

12654029

R.Boldt, and R.Zrenner (2003).
Purine and pyrimidine biosynthesis in higher plants.

Physiol Plant, 117, 297-304.

9611179

D.Guyer, A.Tuttle, S.Rouse, S.Volrath, M.Johnson, S.Potter, J.Görlach, S.Goff, L.Crossland, and E.Ward (1998).
Activation of latent transgenes in Arabidopsis using a hybrid transcription factor.

Genetics, 149, 633-639.

9568898

M.Gregoriou, M.E.Noble, K.A.Watson, E.F.Garman, T.M.Krulle, C.de la Fuente, G.W.Fleet, N.G.Oikonomakos, and L.N.Johnson (1998).
The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding.

Protein Sci, 7, 915-927.

PDB codes:

1a8i 2gpn

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.