Nakamura Tsutomu, Mine Shouhei, Hagihara Yoshihisa, Ishikawa Kazuhiko, Uegaki Koichi
National Institute of Advanced Industrial Science and Technology, Ikeda, Osaka 563-8577, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt 1):7-11. doi: 10.1107/S1744309106051773. Epub 2006 Dec 16.
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.
嗜热古菌激烈火球菌(Pyrococcus furiosus)几丁质酶催化结构域(AD2(PF-ChiA))的晶体结构已在1.5埃分辨率下确定。这是古菌几丁质酶催化结构域的首个结构。AD2(PF-ChiA)的整体结构是一个TIM桶状折叠,带有一个隧道状活性位点,这是18家族几丁质酶的共同特征。尽管催化残基(Asp522、Asp524和Glu526)是保守的,但将保守残基和结构与其他同源几丁质酶进行比较表明,PF-ChiA的催化机制与18家族几丁质酶不同。