3IWD

T. maritima AdoMetDC complex with 5'-Deoxy-5'-dimethyl thioadenosine

3IWD の概要

• エントリーDOI: 10.2210/pdb3iwd/pdb
• 関連するPDBエントリー: 1TLU 1TMI
• 分子名称: S-adenosylmethionine decarboxylase, 5'-deoxy-5'-(dimethyl-lambda~4~-sulfanyl)adenosine, ... (4 entities in total)
• 機能のキーワード: autocatalytic cleavage, decarboxylase, lyase, polyamine biosynthesis, pyruvate, s-adenosyl-l-methionine, schiff base, spermidine biosynthesis, zymogen
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 30242.18

構造登録者

Bale, S.,Kavita, B.,Ealick, S.E. (登録日: 2009-09-02, 公開日: 2010-02-09, 最終更新日: 2024-10-16)

主引用文献

Bale, S.,Baba, K.,McCloskey, D.E.,Pegg, A.E.,Ealick, S.E.
Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity.
Acta Crystallogr.,Sect.D, 66:181-189, 2010

PubMed Abstract: The polyamines putrescine, spermidine and spermine are ubiquitous aliphatic cations and are essential for cellular growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. The crystal structures of AdoMetDC from humans and plants and of the AdoMetDC proenzyme from Thermotoga maritima have been obtained previously. Here, the crystal structures of activated T. maritima AdoMetDC (TmAdoMetDC) and of its complexes with S-adenosylmethionine methyl ester and 5'-deoxy-5'-dimethylthioadenosine are reported. The results demonstrate for the first time that TmAdoMetDC autoprocesses without the need for additional factors and that the enzyme contains two complete active sites, both of which use residues from both chains of the homodimer. The complexes provide insights into the substrate specificity and ligand binding of AdoMetDC in prokaryotes. The conservation of the ligand-binding mode and the active-site residues between human and T. maritima AdoMetDC provides insight into the evolution of AdoMetDC.

PubMed: 20124698
DOI: 10.1107/S090744490904877X

実験手法

X-RAY DIFFRACTION (1.9 Å)