Crystal Structure of yHst2 bound to the intermediate analogue ADP-HPD, and and aceylated H4 peptide

Structural basis for nicotinamide inhibition and base exchange in sir2 enzymes.

Hst2 catalytic core domain, residues 1-294

MRGSHHHHHHGMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGISTSCGIPDFRSPGTGLYHNLARLKLPYPEAV
FDVDFFQSDPLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQNIDTLERQAGVKDDLIIEAHGSFAHCHCIGC
GKVYPPQVFKSKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSETWLNDSEWLREKITTSGKHPQQPLVIVVGTSL
AVYPFASLPEEIPRKVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEELGWQEDFEKILTAQ

2.0 M Ammonium Sulfate, 0.1 M sodium citrate, 0.2 M potassium/sodium tartrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

yHst2 bound to carba-NAD+ and an acetylated H4 peptide

yHst2 bound to ADP-Ribose and an acetylated H4 peptide

Crystal Structure of yHst2 I117F mutant bound to carba-NAD+ and an acetylated H4 peptide

The biological assembly is a trimer generated from the monomer in the asymmetric unit.

Zn binding domain, Rossmann fold, HYDROLASE

MSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGISTSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQSDPLPFY
TLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQNIDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQVFKSKLA
EHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSETWLNDSEWLREKITTSGKHPQQPLVIVVGTSLAVYPFASLPEEIPR
KVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEELGWQEDFEKILTAQ