Structural analysis of thermostable S. solfataricus purine-specific nucleoside hydrolase

New Determinants in the Catalytic Mechanism of Nucleoside Hydrolases from the Structures of Two Isozymes from Sulfolobus solfataricus.

Biochemical characterization and homology modeling of a purine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus: insights into mechanisms of protein stabilization.

MRKVIVDSDTATDDTIAILLASRFFQLLGVTIVAGNVNYNQEVKNALFTLEYIGKQDVPVYLGSQRPILGNWRTVEEVHG
SNGMSNWNYPEPNKRPEKEHAIDAILRLSKEHEGELEILAISPLTNIALAYLKDPSVVKRVKKIWIMGGAFSKGNTTPIA
EFNFWVDPEAAKIVLDAGFDITIVPWEVAEISGSLNERDWEYISKLNTKLSNFFINVNKTLKEYTTKNQGISGSIHPDSL
TVSIAHDNSIILDSSLKYVDVELCSKSRGAMLIDWYSLHKNKPNAEIVLKADGGKFKNLLFNSLSQ

100 mM HEPES, 5% PEG 3350, 5 mM CaCl2, 5 mM CdCl2, 5 mM MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; U VALUES: REFINED INDIVIDUALLY

Purine nucleoside hydrolase, thermostable protein, Open (alpha, beta) structure, Rossmann fold, NH-fold, nucleoside hydrolase, Nucleotide metabolism, N-glycosidase, HYDROLASE