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

Protein Sci. 2005 Mar;14(3):823-7. doi: 10.1110/ps.041229405. Epub 2005 Feb 2.

Abstract

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 A 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 beta sheet surrounded by four alpha-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Pentosyltransferases / chemistry*
  • Pentosyltransferases / genetics
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Thermus thermophilus / enzymology*
  • Thermus thermophilus / genetics

Substances

  • Bacterial Proteins
  • Pentosyltransferases
  • uracil phosphoribosyltransferase