PDBsum entry: 1gyh

Hydrolase

PDB-id: 1gyh

Main view

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

318 a.a. *

Metal ions

_CL ×6

Waters ×1910

* Residue conservation analysis

Tools

Clefts Calculation

Bottom view	Right view

PDB id:

1gyh

Name:

Hydrolase

Title:

Structure of d158a cellvibrio cellulosa alpha-l-arabinanase mutant

Structure:

Arabinan endo-1,5-alpha-l-arabinosidase a. Chain: a, b, c, d, e, f. Synonym: alpha-l-arabinanase, abn a, endo-1,5-alpha-l-arabinanase a. Engineered: yes. Mutation: yes. Other_details: engineered mutation asp 158 ala

Source:

Cellvibrio cellulosa. Organism_taxid: 155077. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: tuner.

UniProt:

Chains A, B, C, D, E, F: P95470 (P95470_9GAMM)

Seq:

Struc:

Seq:

347 a.a.

Struc:

318 a.a.*

Key:	PfamA domain
Secondary structure	CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme class:

E.C.3.2.1.99   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

Endohydrolysis of 1,5-alpha-L-arabinofuranosidic linkages in 1,5-arabinans.

Resolution:

1.89Å

R-factor:

0.147

R-free:

0.203

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

Related entries:

1gyd structure of cellvibrio cellulosa alpha-l- arabinanase
1gye structure of d158a cellvibrio cellulosa alpha -l-arabinanase mutant complexed with arabinohexaose

Quick_links

Procheck

Surface

Key reference

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.