PDBsum entry 6a8h

Hydrolase

PDB id: 6a8h

Contents

Protein chain

315 a.a.

Ligands

AHR-AHR-AHR ×2

Metals

_MG

_CA

Waters ×266

PDB id:

6a8h

Name:

Hydrolase

Title:

Crystal structure of endo-arabinanase abn-ts d27a mutant in complex with arabinotriose

Structure:

Endo-alpha-(1->5)-l-arabinanase. Chain: a. Synonym: arabinanase-ts,abn,endo-1,5-alpha-l-arabinanase. Engineered: yes. Mutation: yes

Source:

Geobacillus thermodenitrificans. Organism_taxid: 33940. Gene: abn-ts. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.65Å R-factor: 0.149 R-free: 0.195

Authors:

A.Yamaguchi,T.Tada

Key ref:

A.Yamaguchi et al. (2018). Structures of endo-1,5-α-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides. Acta Crystallogr F Struct Biol Commun, 74, 774-780. PubMed id: 30511671 DOI: 10.1107/S2053230X18015947

Date:

09-Jul-18 Release date: 19-Dec-18

Protein chain

Q93HT9  (IABN_GEOTD) -  Intracellular endo-alpha-(1->5)-L-arabinanase from Geobacillus thermodenitrificans

Seq: 313 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.

DOI no: 10.1107/S2053230X18015947

Acta Crystallogr F Struct Biol Commun 74:774-780 (2018)

PubMed id: 30511671

Structures of endo-1,5-α-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides.

A.Yamaguchi, Y.Sogabe, S.Fukuoka, T.Sakai, T.Tada.

ABSTRACT

The thermostable endo-1,5-α-L-arabinanase from Bacillus thermodenitrificans TS-3 (ABN-TS) hydrolyzes the α-1,5-L-arabinofuranoside linkages of arabinan. In this study, the crystal structures of inactive ABN-TS mutants, D27A and D147N, were determined in complex with arabino-oligosaccharides. The crystal structures revealed that ABN-TS has at least six subsites in the deep V-shaped cleft formed across one face of the propeller structure. The structural features indicate that substrate recognition is profoundly influenced by the remote subsites as well as by the subsites surrounding the active center. The `open' structure of the substrate-binding cleft of the endo-acting ABN-TS is suitable for the random binding of several sugar units in polymeric substrates.