1AD4

DIHYDROPTEROATE SYNTHETASE COMPLEXED WITH OH-CH2-PTERIN-PYROPHOSPHATE FROM STAPHYLOCOCCUS AUREUS

1AD4 の概要

• エントリーDOI: 10.2210/pdb1ad4/pdb
• 分子名称: DIHYDROPTEROATE SYNTHETASE, MANGANESE (II) ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase, synthetase, dihydropteroate synthetase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59401.13

構造登録者

Oefner, C.,Kostrewa, D. (登録日: 1997-02-20, 公開日: 1998-04-29, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)