M.Kataoka
and
K.Ishikawa
(2014).
A new crystal form of a hyperthermophilic endocellulase.
Acta Crystallogr F Struct Biol Commun,
70,
878-883.
PubMed id: 25005081
DOI: 10.1107/S2053230X14010930
A new crystal form of a hyperthermophilic endocellulase.
M.Kataoka,
K.Ishikawa.
ABSTRACT
The hyperthermophilic glycoside hydrolase family endocellulase 12 from the
archaeon Pyrococcus furiosus (EGPf; Gene ID PF0854; EC 3.2.1.4) catalyzes the
hydrolytic cleavage of the β-1,4-glucosidic linkage in β-glucan in
lignocellulose biomass. A crystal of EGPf was previously prepared at pH 9.0 and
its structure was determined at an atomic resolution of 1.07 Å. This article
reports the crystallization of EGPf at the more physiologically relevant pH of
5.5. Structure determination showed that this new crystal form has the symmetry
of space group C2. Two molecules of the enzyme are observed in the asymmetric
unit. Crystal packing is weak at pH 5.5 owing to two flexible interfaces between
symmetry-related molecules. Comparison of the EGPf structures obtained at pH 9.0
and pH 5.5 reveals a significant conformational difference at the active centre
and in the surface loops. The interfaces in the vicinity of the flexible surface
loops impact the quality of the EGPf crystal.
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