1GYH

Structure of D158A Cellvibrio cellulosa alpha-L-arabinanase mutant

Summary for 1GYH

• Entry DOI: 10.2210/pdb1gyh/pdb
• Related: 1GYD 1GYE
• Descriptor: ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE A, CHLORIDE ION (3 entities in total)
• Functional Keywords: arabinanase, hydrolase, propeller, catalysis, cellvibrio, pseudomonas
• Biological source: CELLVIBRIO CELLULOSA
• Total number of polymer chains: 6
• Total formula weight: 217091.79

Authors

Nurizzo, D.,Turkenburg, J.P.,Charnock, S.J.,Roberts, S.M.,Dodson, E.J.,McKie, V.A.,Taylor, E.J.,Gilbert, H.J.,Davies, G.J. (deposition date: 2002-04-23, release date: 2002-08-23, Last modification date: 2024-05-01)

Primary citation

Nurizzo, D.,Turkenburg, J.P.,Charnock, S.J.,Roberts, S.M.,Dodson, E.J.,Mckie, V.A.,Taylor, E.J.,Gilbert, H.J.,Davies, G.J.
Cellovibrio Cellulosa Alpha-L-Arabinanase 43A Has a Novel Five-Blade Beta-Propeller Fold
Nat.Struct.Biol., 9:665-, 2002

PubMed 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.

PubMed: 12198486
DOI: 10.1038/NSB835

Experimental method

X-RAY DIFFRACTION (1.89 Å)