| Literature DB >> 17183162 |
Tsutomu Nakamura1, Shouhei Mine, Yoshihisa Hagihara, Kazuhiko Ishikawa, Koichi Uegaki.
Abstract
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.Entities:
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Year: 2006 PMID: 17183162 PMCID: PMC2330115 DOI: 10.1107/S1744309106051773
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091