Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana

Catalyzing the first step in the de novo synthesis of adenylmonophosphate, adenylosuccinate synthetase (AdSS) is a known target for herbicides and antibiotics. We have purified and crystallized recombinant AdSS from Arabidopsis thaliana and Tritium aestivum, expressed in Escherichia coli. The struct...

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Bibliographic Details
Published in:Journal of molecular biology 2000-02, Vol.296 (2), p.569-577
Main Authors: Prade, L, Cowan-Jacob, S.W, Chemla, P, Potter, S, Ward, E, Fonne-Pfister, R
Format: Article
Language:English
Subjects:
Adenylosuccinate Synthase - chemistry
Adenylosuccinate Synthase - genetics
Adenylosuccinate Synthase - metabolism
Amino Acid Sequence
Arabidopsis - enzymology
Arabidopsis thaliana
Binding Sites
crystal structure
Crystallography, X-Ray
crystals
Dimerization
Escherichia coli - enzymology
Escherichia coli - genetics
guanosine diphosphate
Guanosine Diphosphate - metabolism
Hydrogen Bonding
Inosine Monophosphate - metabolism
Ligands
ligases
Models, Molecular
molecular conformation
Molecular Sequence Data
pdb/1dj2
pdb/1dj3
Protein Folding
protein secondary structure
Protein Structure, Secondary
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Alignment
Static Electricity
Triticum - enzymology
Triticum aestivum
X-ray diffraction
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Description
Summary:Catalyzing the first step in the de novo synthesis of adenylmonophosphate, adenylosuccinate synthetase (AdSS) is a known target for herbicides and antibiotics. We have purified and crystallized recombinant AdSS from Arabidopsis thaliana and Tritium aestivum, expressed in Escherichia coli. The structures of A. thaliana and T. aestivum AdSS in complex with GDP were solved at 2.9 A and 3.0 A resolution, respectively. Comparison with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein. The longer N terminus in the plant sequences is at the same place as the longer C terminus of the E. coli sequence in the 3D structure. The GDP-binding sites have one additional hydrogen-bonding partner, which is a plausible explanation for the lower K(m) value. Due to its special position, this partner may also enable GTP to initiate a conformational change, which was, in E. coli AdSS, exclusively activated by ligands at the IMP-binding site. The dimer interfaces show up to six hydrogen bonds and six salt-bridges more than in the E. coli structure, although the contact areas have approximately the same size.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1999.3473