5JTS
Structure of a beta-1,4-mannanase, SsGH134.
Summary for 5JTS
| Entry DOI | 10.2210/pdb5jts/pdb |
| Descriptor | beta-1,4-mannanase, GLYCEROL, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | beta-1, 4-mannanase, carbohydrate degrading, glycosyl hydrolase, hydrolase |
| Biological source | Streptomyces sp. nrrl B-244 |
| Total number of polymer chains | 1 |
| Total formula weight | 18378.54 |
| Authors | Jin, Y.,Petricevic, M.,Goddard-Borger, E.D.,Williams, S.J.,Davies, G.J. (deposition date: 2016-05-09, release date: 2016-11-16, Last modification date: 2024-11-20) |
| Primary citation | Jin, Y.,Petricevic, M.,John, A.,Raich, L.,Jenkins, H.,Portela De Souza, L.,Cuskin, F.,Gilbert, H.J.,Rovira, C.,Goddard-Borger, E.D.,Williams, S.J.,Davies, G.J. A beta-Mannanase with a Lysozyme-like Fold and a Novel Molecular Catalytic Mechanism. ACS Cent Sci, 2:896-903, 2016 Cited by PubMed Abstract: The enzymatic cleavage of β-1,4-mannans is achieved by -β-1,4-mannanases, enzymes involved in germination of seeds and microbial hemicellulose degradation, and which have increasing industrial and consumer product applications. β-Mannanases occur in a range of families of the CAZy sequence-based glycoside hydrolase (GH) classification scheme including families 5, 26, and 113. In this work we reveal that β-mannanases of the newly described GH family 134 differ from other mannanase families in both their mechanism and tertiary structure. A representative GH family 134 -β-1,4-mannanase from a sp. displays a fold closely related to that of hen egg white lysozyme but acts with inversion of stereochemistry. A Michaelis complex with mannopentaose, and a product complex with mannotriose, reveal ligands with pyranose rings distorted in an unusual inverted chair conformation. quantum mechanics/molecular mechanics metadynamics quantified the energetically accessible ring conformations and provided evidence in support of a → → conformational itinerary along the reaction coordinate. This work, in concert with that on GH family 124 cellulases, reveals how the lysozyme fold can be co-opted to catalyze the hydrolysis of different polysaccharides in a mechanistically distinct manner. PubMed: 28058278DOI: 10.1021/acscentsci.6b00232 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.09 Å) |
Structure validation
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