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Structure of a UPF0150‐family protein from Thermus thermophilus HB8
Author(s) -
Okazaki Nobuo,
Kumei Maki,
Manzoku Miho,
Kuramitsu Seiki,
Shirouzu Mikako,
Shinkai Akeo,
Yokoyama Shigeyuki
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107006070
Subject(s) - thermus thermophilus , homotetramer , rna , crystallography , protein structure , hypothetical protein , chemistry , biology , computational biology , genetics , biochemistry , gene , escherichia coli , protein subunit
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.

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