6A8H
Crystal structure of endo-arabinanase ABN-TS D27A mutant in complex with arabinotriose
Summary for 6A8H
| Entry DOI | 10.2210/pdb6a8h/pdb |
| Descriptor | endo-alpha-(1->5)-L-arabinanase, alpha-L-arabinofuranose-(1-5)-alpha-L-arabinofuranose-(1-5)-alpha-L-arabinofuranose, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | arabinanase, thermostable enzyme, glycoside hydrolase, gh43, hydrolase |
| Biological source | Geobacillus thermodenitrificans |
| Total number of polymer chains | 1 |
| Total formula weight | 37407.82 |
| Authors | Yamaguchi, A.,Tada, T. (deposition date: 2018-07-09, release date: 2018-12-19, Last modification date: 2023-11-22) |
| Primary citation | 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, 74:774-780, 2018 Cited by PubMed 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. PubMed: 30511671DOI: 10.1107/S2053230X18015947 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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