1YAK

Complex of Bacillus subtilis TenA with 4-amino-2-methyl-5-hydroxymethylpyrimidine

1YAK の概要

• エントリーDOI: 10.2210/pdb1yak/pdb
• 関連するPDBエントリー: 1YAD 1YAF
• 分子名称: Transcriptional activator tenA, 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE (3 entities in total)
• 機能のキーワード: thiaminase, transcription
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122836.61

構造登録者

Toms, A.V.,Haas, A.L.,Park, J.-H.,Begley, T.P.,Ealick, S.E. (登録日: 2004-12-17, 公開日: 2005-02-22, 最終更新日: 2023-08-23)

主引用文献

Toms, A.V.,Haas, A.L.,Park, J.H.,Begley, T.P.,Ealick, S.E.
Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II.
Biochemistry, 44:2319-2329, 2005

PubMed Abstract: Bacillus subtilis gene products TenA and TenI have been implicated in regulating the production of extracellular proteases, but their role in the regulation process remains unclear. The structural characterization of these proteins was undertaken to help provide insight into their function. We have determined the structure of TenA alone and in complex with 4-amino-2-methyl-5-hydroxymethylpyrimidine, and we demonstrate that TenA is a thiaminase II. The TenA structure suggests that the degradation of thiamin by TenA likely proceeds via the same addition-elimination mechanism described for thiaminase I. Three active-site residues, Asp44, Cys135, and Glu205, are likely involved in substrate binding and catalysis based on the enzyme/product complex structure and the conservation of these residues within TenA sequences. We have also determined the structure of TenI. Although TenI shows significant structural homology to thiamin phosphate synthase, it has no known enzymatic function. The structure suggests that TenI is unable to bind thiamin phosphate, largely resulting from the presence of leucine at position 119, while the corresponding residue in thiamin phosphate synthase is glycine.

PubMed: 15709744
DOI: 10.1021/bi0478648

実験手法

X-RAY DIFFRACTION (2.5 Å)