3FPG

Crystal Structure of E81Q mutant of MtNAS

3FPG の概要

• エントリーDOI: 10.2210/pdb3fpg/pdb
• 関連するPDBエントリー: 3FPE 3FPF 3FPH 3FPJ
• 分子名称: Putative uncharacterized protein, BROMIDE ION, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: thermonicotianamine, nicotianamine, biosynthetic protein, transferase
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68061.71

構造登録者

Dreyfus, C.,Pignol, D.,Arnoux, P. (登録日: 2009-01-05, 公開日: 2009-10-06, 最終更新日: 2024-11-06)

主引用文献

Dreyfus, C.,Lemaire, D.,Mari, S.,Pignol, D.,Arnoux, P.
Crystallographic snapshots of iterative substrate translocations during nicotianamine synthesis in Archaea
Proc.Natl.Acad.Sci.USA, 106:16180-16184, 2009

PubMed Abstract: Nicotianamine (NA), a small molecule ubiquitous in plants, is an important divalent metal chelator and the main precursor of phytosiderophores. Nicotianamine synthase (NAS) is the enzyme catalyzing NA synthesis by the condensation of three aminopropyl moieties of S-adenosylmethionine (SAM) and the cyclization of one of them to form an azetidine ring. Here we report five crystal structures of an archaeal NAS from Methanothermobacter thermautotrophicus, either free or in complex with its product(s) and substrate(s). These structures reveal a two-domains fold arrangement of MtNAS, a small molecule related to NA (named here thermoNicotianamine or tNA), and an original mechanism of synthesis in a buried reaction chamber. This reaction chamber is open to the solvent through a small inlet, and a single active site allows the selective entrance of only one substrate at a time that is then processed and translocated stepwise.

PubMed: 19805277
DOI: 10.1073/pnas.0904439106

実験手法

X-RAY DIFFRACTION (2 Å)