Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)


structural genomics communications



Acta Cryst. (2007). F63, 173-177    [ doi:10.1107/S1744309107006070 ]

Structure of a UPF0150-family protein from Thermus thermophilus HB8

N. Okazaki, M. Kumei, M. Manzoku, S. Kuramitsu, M. Shirouzu, A. Shinkai and S. Yokoyama

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 Å 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.

PDB reference: 2dsy

Keywords: [alpha]-[beta]-[beta]-[beta]-[alpha] fold; COG1598; hypothetical protein; Thermus thermophilus; UPF0150.

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