Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.,Nakamura T, Mine S, Hagihara Y, Ishikawa K, Uegaki K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):7-11. Epub 2006 Dec 16. PMID:17183162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nakamura T, Mine S, Hagihara Y, Ishikawa K, Uegaki K. Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):7-11. Epub 2006 Dec 16. PMID:17183162 doi:10.1107/S1744309106051773
