1dj3
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(New page: 200px<br /><applet load="1dj3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dj3, resolution 3.0Å" /> '''STRUCTURES OF ADENYLO...)
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Revision as of 11:12, 20 November 2007
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STRUCTURES OF ADENYLOSUCCINATE SYNTHETASE FROM TRITICUM AESTIVUM AND ARABIDOPSIS THALIANA
Overview
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.
About this Structure
1DJ3 is a Single protein structure of sequence from Triticum aestivum with GDP as ligand. Active as Adenylosuccinate synthase, with EC number 6.3.4.4 Full crystallographic information is available from OCA.
Reference
Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana., Prade L, Cowan-Jacob SW, Chemla P, Potter S, Ward E, Fonne-Pfister R, J Mol Biol. 2000 Feb 18;296(2):569-77. PMID:10669609
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