1GYD
Structure of Cellvibrio cellulosa alpha-L-arabinanase
Summary for 1GYD
Entry DOI | 10.2210/pdb1gyd/pdb |
Related | 1GYE 1GYH |
Descriptor | ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE A (2 entities in total) |
Functional Keywords | arabinanase, hydrolase, propeller, catalysis, cellvibrio, pseudomonas |
Biological source | CELLVIBRIO CELLULOSA |
Total number of polymer chains | 1 |
Total formula weight | 35933.21 |
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: 2024-10-16) |
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. Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nat. Struct. Biol., 9:665-668, 2002 Cited by 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: 12198486DOI: 10.1038/nsb835 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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