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Updated: Jul 16, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Structure of a UPF0150-family protein from Thermus thermophilus HB8
Nobuo Okazaki1, Maki Kumei, Miho Manzoku
1RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148, Japan.
Abstract:
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 A resolution to a final R factor of 18.5%. The TTHA0281 monomer adopts an alpha-beta-beta-beta-alpha 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.
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