1DHN

1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS

1DHN の概要

• エントリーDOI: 10.2210/pdb1dhn/pdb
• 分子名称: 7,8-DIHYDRONEOPTERIN ALDOLASE (2 entities in total)
• 機能のキーワード: pterin binding, folate biosynthesis, antibiotic target, beta-barrel
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13769.64

構造登録者

Hennig, M.,D'Arcy, A.,Hampele, I.C.,Page, M.G.P.,Oefner, C.H.,Dale, G. (登録日: 1998-03-31, 公開日: 1999-04-20, 最終更新日: 2024-02-07)

主引用文献

Hennig, M.,D'Arcy, A.,Hampele, I.C.,Page, M.G.,Oefner, C.,Dale, G.E.
Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus.
Nat.Struct.Biol., 5:357-362, 1998

PubMed Abstract: Dihydroneopterin aldolase catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin during the de novo synthesis of folic acid from guanosine triphosphate. The gene encoding the dihydroneopterin aldolase from S. aureus has been cloned, sequenced and expressed in Escherichia coli. The protein has been purified for biochemical characterization and its X-ray structure determined at 1.65 A resolution. The protein forms an octamer of 110,000 Mr molecular weight. Four molecules assemble into a ring, and two rings come together to give a cylinder with a hole of at least 13 A diameter. The structure of the binary complex with the product 6-hydroxymethyl-7,8-dihydropterin has defined the location of the active site. The structural information and results of site directed mutagenesis allow an enzyme reaction mechanism to be proposed.

PubMed: 9586996
DOI: 10.1038/nsb0598-357

実験手法

X-RAY DIFFRACTION (1.65 Å)