1rtw

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spinqualitylabelsall models 1rtw, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1RTW is a Single protein structure of sequence from Pyrococcus furiosus dsm 3638 with PO4 and MP5 as ligands. Full crystallographic information is available from OCA.

Reference

The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism., Benach J, Edstrom WC, Lee I, Das K, Cooper B, Xiao R, Liu J, Rost B, Acton TB, Montelione GT, Hunt JF, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):589-98. Epub 2005, Apr 20. PMID:15858269

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