1RTW

X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34

1RTW の概要

• エントリーDOI: 10.2210/pdb1rtw/pdb
• 分子名称: transcriptional activator, putative, (4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL DIHYDROGEN PHOSPHATE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: pf1337, tena, thiamin, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 107550.57

構造登録者

Benach, J.,Edstrom, W.C.,Lee, I.,Rong, X.,Acton, T.B.,Montelione, G.T.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (登録日: 2003-12-10, 公開日: 2004-01-13, 最終更新日: 2024-10-16)

主引用文献

Benach, J.,Edstrom, W.C.,Lee, I.,Das, K.,Cooper, B.,Xiao, R.,Liu, J.,Rost, B.,Acton, T.B.,Montelione, G.T.,Hunt, J.F.
The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism.
Acta Crystallogr.,Sect.D, 61:589-598, 2005

PubMed Abstract: TenA (transcriptional enhancer A) has been proposed to function as a transcriptional regulator based on observed changes in gene-expression patterns when overexpressed in Bacillus subtilis. However, studies of the distribution of proteins involved in thiamine biosynthesis in different fully sequenced genomes have suggested that TenA may be an enzyme involved in thiamine biosynthesis, with a function related to that of the ThiC protein. The crystal structure of PF1337, the TenA homolog from Pyrococcus furiosus, is presented here. The protomer comprises a bundle of alpha-helices with a similar tertiary structure and topology to that of human heme oxygenase-1, even though there is no significant sequence homology. A solvent-sequestered cavity lined by phylogenetically conserved residues is found at the core of this bundle in PF1337 and this cavity is observed to contain electron density for 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate, the product of the ThiC enzyme. In contrast, the modestly acidic surface of PF1337 shows minimal levels of sequence conservation and a dearth of the basic residues that are typically involved in DNA binding in transcription factors. Without significant conservation of its surface properties, TenA is unlikely to mediate functionally important protein-protein or protein-DNA interactions. Therefore, the crystal structure of PF1337 supports the hypothesis that TenA homologs have an indirect effect in altering gene-expression patterns and function instead as enzymes involved in thiamine metabolism.

PubMed: 15858269
DOI: 10.1107/S0907444905005147

実験手法

X-RAY DIFFRACTION (2.35 Å)