Open AccessStructure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus
Author(s) -
Nakamura Tsutomu,
Mine Shouhei,
Hagihara Yoshihisa,
Ishikawa Kazuhiko,
Uegaki Koichi
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106051773
Subject(s) - pyrococcus furiosus , chitinase , thermophile , thermostability , archaea , chemistry , catalysis , hydrolase , pyrococcus horikoshii , biochemistry , crystallography , enzyme , gene
The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2 PF‐ChiA ) has been determined at 1.5 Å resolution. This is the first structure of the catalytic domain of an archaeal chitinase. The overall structure of AD2 PF‐ChiA is a TIM‐barrel fold with a tunnel‐like active site that is a common feature of family 18 chitinases. Although the catalytic residues (Asp522, Asp524 and Glu526) are conserved, comparison of the conserved residues and structures with those of other homologous chitinases indicates that the catalytic mechanism of PF‐ChiA is different from that of family 18 chitinases.