Nurizzo, Didier and Turkenburg, Johan P. and Charnock, Simon J. and Roberts, Shirley M. and Dodson, Eleanor J. and McKie, Vincent A. and Taylor, Edward J. and Gilbert, Harry J. and Davies, Gideon J. (2002) Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nature Structural Biology, 9 (9). pp. 665-668. ISSN 1072-8368

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Abstract

Cellvibrio japonicus arabinanase Arb43A hydrolyzes the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 A resolution, reveals a five-bladed beta-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.

Item Type:	Article
Additional Information:	Cellvibrio japonicus arabinanase Arb43A hydrolyzes the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 A resolution, reveals a five-bladed beta-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.
Keywords:	Arb43A, alpha-1, 5-linked L-arabinofuranoside, five-bladed beta-propeller fold
Subjects:	C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
Divisions:	College of Sciences > Faculty of Science > School of Life Sciences
Depositing User:	Edward Taylor
Date Deposited:	18 Sep 2012 20:25
Last Modified:	13 Mar 2013 09:13
URI:	http://eprints.lincoln.ac.uk/id/eprint/6180

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