Crystal structure of a predicted phosphoribosyltransferase (TT1426) from Thermus thermophilus HB8 at 2.01 Å resolution

Mutsuko Kukimoto-Niino, Rie Shibata, Kazutaka Murayama, Hiroaki Hamana, Madoka Nishimoto, Yoshitaka Bessho, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


TT1426, from Thermus thermophilus HB8, is a conserved hypothetical protein with a predicted phosphoribosyltransferase (PRTase) domain, as revealed by a Pfam database search. The 2.01 Å crystal structure of TT1426 has been determined by the multiwavelength anomalous dispersion (MAD) method. TT1426 comprises a core domain consisting of a central five-stranded β sheet surrounded by four α-helices, and a subdomain in the C terminus. The core domain structure resembles those of the type I PRTase family proteins, although a significant structural difference exists in an inserted 43-residue region. The C-terminal subdomain corresponds to the "hood," which contains a substrate-binding site in the type I PRTases. The hood structure of TT1426 differs from those of the other type I PRTases, suggesting the possibility that TT1426 binds an unknown substrate. The structure-based sequence alignment provides clues about the amino acid residues involved in catalysis and substrate binding.

Original languageEnglish
Pages (from-to)823-827
Number of pages5
JournalProtein Science
Issue number3
Publication statusPublished - 2005 Mar
Externally publishedYes


  • Hypothetical protein
  • Phosphoribosyltransferase
  • Structural genomics
  • Thermus thermophilus

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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