1ZUD

Structure of ThiS-ThiF protein complex

1ZUD の概要

• エントリーDOI: 10.2210/pdb1zud/pdb
• 分子名称: Adenylyltransferase thiF, ThiS protein, ZINC ION, ... (6 entities in total)
• 機能のキーワード: thiamin, thiazole, protein-protein complex, this, thif, transferase-biosynthetic protein complex, transferase/biosynthetic protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68870.85

構造登録者

Ealick, S.E.,Lehmann, C. (登録日: 2005-05-30, 公開日: 2006-01-31, 最終更新日: 2023-08-23)

主引用文献

Lehmann, C.,Begley, T.P.,Ealick, S.E.
Structure of the Escherichia coli ThiS-ThiF Complex, a Key Component of the Sulfur Transfer System in Thiamin Biosynthesis.
Biochemistry, 45:11-19, 2006

PubMed Abstract: We have determined the crystal structure of the Escherichia coli ThiS-ThiF protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins involved in the synthesis of the thiazole moiety of thiamin. ThiF catalyzes the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation. ThiS is a small 7.2 kDa protein that structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD. ThiF is a 27 kDa protein with distinct sequence and structural similarity to the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies the mechanism of the sulfur transfer chemistry involved in thiazole biosynthesis.

PubMed: 16388576
DOI: 10.1021/bi051502y

実験手法

X-RAY DIFFRACTION (1.98 Å)