1Q0N

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM E. COLI WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.25 ANGSTROM RESOLUTION

「1EQO」から置き換えられました

1Q0N の概要

• エントリーDOI: 10.2210/pdb1q0n/pdb
• 関連するPDBエントリー: 1CBK 1DY3 1EQ0 1EQM 1EQO 1EX8 1F9H 1F9Y 1G4C 1HKA 1HQ2 1IM6 1KBR
• 分子名称: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: pyrophosphokinase, pyrophosphoryl transfer, folate, hppk, pterin, 6-hydroxymethyl-7, 8-dihydropterin, ternary complex, substrate specificity, antimicrobial agent, drug design, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18987.16

構造登録者

Blaszczyk, J.,Ji, X. (登録日: 2003-07-16, 公開日: 2003-08-26, 最終更新日: 2023-08-30)

主引用文献

Blaszczyk, J.,Shi, G.,Yan, H.,Ji, X.
Catalytic Center Assembly of Hppk as Revealed by the Crystal Structure of a Ternary Complex at 1.25 A Resolution
Structure, 8:1049-1058, 2000

PubMed Abstract: Folates are essential for life. Unlike mammals, most microorganisms must synthesize folates de novo. 6-Hydroxymethyl-7, 8-dihydropterin pyrophosphokinase (HPPK) catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate pathway, and therefore is an ideal target for developing novel antimicrobial agents. HPPK from Escherichia coli is a 158-residue thermostable protein that provides a convenient model system for mechanistic studies. Crystal structures have been reported for HPPK without bound ligand, containing an HP analog, and complexed with an HP analog, two Mg(2+) ions, and ATP.

PubMed: 11080626
DOI: 10.1016/S0969-2126(00)00502-5

実験手法

X-RAY DIFFRACTION (1.25 Å)