Format

Send to

Choose Destination
Nat Struct Biol. 2002 Sep;9(9):665-8.

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

Author information

1
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, UK.

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.

PMID:
12198486
DOI:
10.1038/nsb835
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center