PDBsum entry: 1gyd

Arabinanase

PDB id: 1gyd

Contents

Protein chain

315 a.a. *

Waters ×184

* Residue conservation analysis

PDB id:

1gyd

Name:

Arabinanase

Title:

Structure of cellvibrio cellulosa alpha-l-arabinanase

Structure:

Arabinan endo-1,5-alpha-l-arabinosidase a. Chain: b. Synonym: alpha-l-arabinanase, abn a, endo-1,5-alpha-l-arabi engineered: yes

Source:

Cellvibrio cellulosa. Organism_taxid: 155077. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21(plyss).

Biol. unit:

Monomer (from PDB file)

Resolution:

2.05Å R-factor: 0.207 R-free: 0.245

Authors:

D.Nurizzo,J.P.Turkenburg,S.J.Charnock,S.M.Roberts,E.J.Dodson V.A.Mckie,E.J.Taylor,H.J.Gilbert,G.J.Davies

Key ref:

D.Nurizzo et al. (2002). Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nat Struct Biol, 9, 665-668. PubMed id: 12198486 DOI: 10.1038/nsb835

Date:

23-Apr-02 Release date: 23-Aug-02

Protein chain

P95470  (P95470_9GAMM) -  Endo-a1,5-arabinanase

Seq: 347 a.a.

Struc: 315 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.2.1.99 - Arabinan endo-1,5-alpha-L-arabinosidase.
• Reaction: Endohydrolysis of 1,5-alpha-L-arabinofuranosidic linkages in 1,5-arabinans.

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (2 terms)
• Biochemical function: hydrolase activity (4 terms)

DOI no: 10.1038/nsb835

Nat Struct Biol 9:665-668 (2002)

PubMed id: 12198486

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

D.Nurizzo, J.P.Turkenburg, S.J.Charnock, S.M.Roberts, E.J.Dodson, V.A.McKie, E.J.Taylor, H.J.Gilbert, G.J.Davies.

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.

Selected figure(s)

Figure 1.
Figure 1. Comparison of the three-dimensional structure of Arb43A and tachylectin. a, Three-dimensional structure of Arb43A in divergent stereo view. The color is 'ramped' from N (blue) to C (green) terminus. The central ion is shown as a sphere. b, The dimer of Arb43A. The orientation of the two monomers suggests that each molecule of the dimer acts on a different substrate chain. c, The structure of tachylectin with the five ligands shown in ball-and-stick representation.

Figure 2.
Figure 2. The reaction catalyzed by Arb43A. The hydrolysis of -1,5-L-arabinans occurs with inversion of anomeric configuration.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2002, 9, 665-668) copyright 2002.

Figures were selected by an automated process.