Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.
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 A 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.
Nakamura
Tsutomu
T
National Institute of Advanced Industrial Science and Technology, Ikeda, Osaka 563-8577, Japan.
Mine
Shouhei
S
Hagihara
Yoshihisa
Y
Ishikawa
Kazuhiko
K
Uegaki
Koichi
K
D000595:Amino Acid Sequence; D020134:Catalytic Domain / Q000235:genetics*; D002688:Chitinases / Q000737:chemistry* / Q000235:genetics*; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary / Q000235:genetics; D020027:Pyrococcus furiosus / Q000201:enzymology* / Q000235:genetics* / Q000302:isolation & purification
D002688:Chitinases