Structural highlights
Function
[IABN_GEOTD] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of endo alpha-(1->5)-L-arabinofuranosyl residues in debranched arabinan.[1]
Publication Abstract from PubMed
The thermostable endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3 (ABN-TS) hydrolyzes the alpha-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.
Structures of endo-1,5-alpha-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides.,Yamaguchi A, Sogabe Y, Fukuoka S, Sakai T, Tada T Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):774-780. doi:, 10.1107/S2053230X18015947. Epub 2018 Nov 26. PMID:30511671[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takao M, Yamaguchi A, Yoshikawa K, Terashita T, Sakai T. Molecular cloning of the gene encoding thermostable endo-1,5-alpha-L-arabinase of Bacillus thermodenitrificans TS-3 and its expression in Bacillus subtilis. Biosci Biotechnol Biochem. 2002 Feb;66(2):430-3. PMID:11999422
- ↑ Yamaguchi A, Sogabe Y, Fukuoka S, Sakai T, Tada T. Structures of endo-1,5-alpha-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides. Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):774-780. doi:, 10.1107/S2053230X18015947. Epub 2018 Nov 26. PMID:30511671 doi:http://dx.doi.org/10.1107/S2053230X18015947
