TY - JOUR
T1 - Crystal structure of a predicted phosphoribosyltransferase (TT1426) from Thermus thermophilus HB8 at 2.01 Å resolution
AU - Kukimoto-Niino, Mutsuko
AU - Shibata, Rie
AU - Murayama, Kazutaka
AU - Hamana, Hiroaki
AU - Nishimoto, Madoka
AU - Bessho, Yoshitaka
AU - Terada, Takaho
AU - Shirouzu, Mikako
AU - Kuramitsu, Seiki
AU - Yokoyama, Shigeyuki
PY - 2005/3
Y1 - 2005/3
N2 - 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.
AB - 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.
KW - Hypothetical protein
KW - Phosphoribosyltransferase
KW - Structural genomics
KW - Thermus thermophilus
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U2 - 10.1110/ps.041229405
DO - 10.1110/ps.041229405
M3 - Article
C2 - 15689504
AN - SCOPUS:20044392105
VL - 14
SP - 823
EP - 827
JO - Protein Science
JF - Protein Science
SN - 0961-8368
IS - 3
ER -