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 (AD2PF‐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 AD2PF‐ChiA is a TIM‐barrel...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-01, Vol.63 (1), p.7-11
Main Authors: Nakamura, Tsutomu, Mine, Shouhei, Hagihara, Yoshihisa, Ishikawa, Kazuhiko, Uegaki, Koichi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Catalytic Domain - genetics
Chitinases - chemistry
Chitinases - genetics
Crystallography, X-Ray
Molecular Sequence Data
Protein Structure Communications
Protein Structure, Secondary - genetics
Pyrococcus furiosus - enzymology
Pyrococcus furiosus - genetics
Pyrococcus furiosus - isolation & purification
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Summary:The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2PF‐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 AD2PF‐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.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309106051773