Cellvibrio japonicus α-L-arabinanase 43A has a novel five-blade β-propeller fold View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-08-19

AUTHORS

Didier Nurizzo, Johan P. Turkenburg, Simon J. Charnock, Shirley M. Roberts, Eleanor J. Dodson, Vincent A. McKie, Edward J. Taylor, Harry J. Gilbert, Gideon J. Davies

ABSTRACT

Cellvibrio japonicus arabinanase Arb43A hydrolyzes the α-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Å resolution, reveals a five-bladed β-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. More... »

PAGES

665-668

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb835

DOI

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

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036765204

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12198486


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