1ad4
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(New page: 200px<br /><applet load="1ad4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ad4, resolution 2.4Å" /> '''DIHYDROPTEROATE SYNTH...)
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Revision as of 08:38, 20 November 2007
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DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS
Overview
The gene encoding the dihydropteroate synthase of staphylococcus aureus, has been cloned, sequenced and expressed in Escherichia coli. The protein, has been purified for biochemical characterization and X-ray, crystallographic studies. The enzyme is a dimer in solution, has a steady, state kinetic mechanism that suggests random binding of the two substrates, and half-site reactivity. The crystal structure of apo-enzyme and a binary, complex with the substrate analogue hydroxymethylpterin pyrophosphate were, determined at 2.2 A and 2.4 A resolution, respectively. The enzyme belongs, to the group of "TIM-barrel" proteins and crystallizes as a, non-crystallographic dimer. Only one molecule of the substrate analogue, bound per dimer in the crystal. Sequencing of nine sulfonamide-resistant, clinical isolates has shown that as many as 14 residues could be involved, in resistance development. The residues are distributed over the surface, of the protein, which defies a simple interpretation of their roles in, resistance. Nevertheless, the three-dimensional structure of the substrate, analogue binary complex could give important insight into the molecular, mechanism of this enzyme.
About this Structure
1AD4 is a Single protein structure of sequence from Staphylococcus aureus with MN, K and HH2 as ligands. Active as Dihydropteroate synthase, with EC number 2.5.1.15 Full crystallographic information is available from OCA.
Reference
Structure and function of the dihydropteroate synthase from Staphylococcus aureus., Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schonfeld HJ, Stuber D, Then RL, J Mol Biol. 1997 Apr 25;268(1):21-30. PMID:9149138
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