2Y5S

Crystal structure of Burkholderia cenocepacia dihydropteroate synthase complexed with 7,8-dihydropteroate.

2Y5S の概要

• エントリーDOI: 10.2210/pdb2y5s/pdb
• 関連するPDBエントリー: 2Y5J
• 分子名称: DIHYDROPTEROATE SYNTHASE, 7,8-DIHYDROPTEROATE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: transferase, folate biosynthesis
• 由来する生物種: BURKHOLDERIA CENOCEPACIA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63697.62

構造登録者

Morgan, R.E.,Batot, G.O.,Dement, J.M.,Rao, V.A.,Eadsforth, T.C.,Hunter, W.N. (登録日: 2011-01-17, 公開日: 2011-01-26, 最終更新日: 2023-12-20)

主引用文献

Morgan, R.E.,Batot, G.O.,Dement, J.M.,Rao, V.A.,Eadsforth, T.C.,Hunter, W.N.
Crystal Structures of Burkholderia Cenocepacia Dihydropteroate Synthase in the Apo-Form and Complexed with the Product 7,8-Dihydropteroate.
Bmc Struct.Biol., 11:21-, 2011

PubMed Abstract: The enzyme dihydropteroate synthase (DHPS) participates in the de novo synthesis of folate cofactors by catalyzing the formation of 7,8-dihydropteroate from condensation of p-aminobenzoic acid with 6-hydroxymethyl-7,8-dihydropteroate pyrophosphate. DHPS is absent from humans, who acquire folates from diet, and has been validated as an antimicrobial therapeutic target by chemical and genetic means. The bacterium Burkholderia cenocepacia is an opportunistic pathogen and an infective agent of cystic fibrosis patients. The organism is highly resistant to antibiotics and there is a recognized need for the identification of new drugs against Burkholderia and related Gram-negative pathogens. Our characterization of the DHPS active site and interactions with the enzyme product are designed to underpin early stage drug discovery.

PubMed: 21554707
DOI: 10.1186/1472-6807-11-21

実験手法

X-RAY DIFFRACTION (1.95 Å)