Structure of a UPF0150-family protein from Thermus thermophilus HB8
- RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148 (Japan)
The crystal structure of the hypothetical protein TTHA0281 from T. thermophilus HB8 has been determined at 1.9 Å resolution. The TTHA0281 protein forms a homotetramer in which each monomer adopts an α-β-β-β-α fold. TTHA0281 is a hypothetical protein from Thermus thermophilus HB8 that belongs to an uncharacterized protein family, UPF0150, in the Pfam database and to COG1598 in the National Center for Biotechnology Information Database of Clusters of Orthologous Groups. The X-ray crystal structure of the protein was determined by a multiple-wavelength anomalous dispersion technique and was refined at 1.9 Å resolution to a final R factor of 18.5%. The TTHA0281 monomer adopts an α-β-β-β-α fold and forms a homotetramer. Based on the properties and functions of structural homologues of the TTHA0281 monomer, the TTHA0281 protein is speculated to be involved in RNA metabolism, including RNA binding and cleavage.
- OSTI ID:
- 22360282
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 3 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8