2DSY

Crystal structure of TTHA0281 from thermus thermophilus HB8

Summary for 2DSY

• Entry DOI: 10.2210/pdb2dsy/pdb
• Descriptor: Hypothetical protein TTHA0281, MAGNESIUM ION, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (4 entities in total)
• Functional Keywords: structural genomics, thermus thermophilus hb8, hypothetical protein, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Total number of polymer chains: 4
• Total formula weight: 39741.31

Authors

Okazaki, N.,Kumei, M.,Shinkai, A.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-07-07, release date: 2007-03-27, Last modification date: 2024-11-06)

Primary citation

Okazaki, N.,Kumei, M.,Manzoku, M.,Kuramitsu, S.,Shirouzu, M.,Shinkai, A.,Yokoyama, S.
Structure of a UPF0150-family protein from Thermus thermophilus HB8
ACTA CRYSTALLOGR.,SECT.F, 63:173-177, 2007

PubMed 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.

PubMed: 17329807
DOI: 10.1107/S1744309107006070

Experimental method

X-RAY DIFFRACTION (1.9 Å)