1AD1

DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS

Summary for 1AD1

• Entry DOI: 10.2210/pdb1ad1/pdb
• Descriptor: DIHYDROPTEROATE SYNTHETASE, POTASSIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: synthetase, transferase, dihydropteroate synthetase, dhps, apo form, complex with oh-ch2-pterin-pyrophosphate
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 59005.33

Authors

Kostrewa, D.,Oefner, C.,D'Arcy, A. (deposition date: 1997-02-19, release date: 1998-04-29, Last modification date: 2024-02-07)

Primary citation

Hampele, I.C.,D'Arcy, A.,Dale, G.E.,Kostrewa, D.,Nielsen, J.,Oefner, C.,Page, M.G.,Schonfeld, H.J.,Stuber, D.,Then, R.L.
Structure and function of the dihydropteroate synthase from Staphylococcus aureus.
J.Mol.Biol., 268:21-30, 1997

PubMed Abstract: 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.

PubMed: 9149138
DOI: 10.1006/jmbi.1997.0944

Experimental method

X-RAY DIFFRACTION (2.2 Å)