ePrints

Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold

Lookup NU author(s): Emeritus Professor Harry Gilbert

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

Cellvibrio japonicus arabinanase Arb43A hydrolyzes the -1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Angstrom 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.

Publication metadata

Author(s): Gilbert HJ; Nurizzo D; Turkenburg JP; Charnock SJ; Roberts SM; Dodson EJ; McKie VA; Taylor EJ; Davies GJ

Publication type: Article

Publication status: Published

Journal: Nature Structural Biology

Year: 2002

Volume: 9

Issue: 9

Pages: 665-668

ISSN (print): 1545-9993

ISSN (electronic):

Publisher: Nature Publishing Group

URL: http://dx.doi.org/10.1038/nsb835

DOI: 10.1038/nsb835

Altmetrics

Share