7D6A
Crystal structure of Oryza sativa Os4BGlu18 monolignol beta-glucosidase
Summary for 7D6A
| Entry DOI | 10.2210/pdb7d6a/pdb |
| Descriptor | Beta-glucosidase 18, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | monolignol beta-glucosidase, os4bglu18, hydrolase |
| Biological source | Oryza sativa subsp. japonica (Rice) |
| Total number of polymer chains | 2 |
| Total formula weight | 112316.71 |
| Authors | Baiya, S.,Pengthaisong, S.,Ketudat Cairns, J.R. (deposition date: 2020-09-29, release date: 2021-01-13, Last modification date: 2024-10-09) |
| Primary citation | Baiya, S.,Pengthaisong, S.,Kitjaruwankul, S.,Ketudat Cairns, J.R. Structural analysis of rice Os4BGlu18 monolignol beta-glucosidase. Plos One, 16:e0241325-e0241325, 2021 Cited by PubMed Abstract: Monolignol glucosides are storage forms of monolignols, which are polymerized to lignin to strengthen plant cell walls. The conversion of monolignol glucosides to monolignols is catalyzed by monolignol β-glucosidases. Rice Os4BGlu18 β-glucosidase catalyzes hydrolysis of the monolignol glucosides, coniferin, syringin, and p-coumaryl alcohol glucoside more efficiently than other natural substrates. To understand more clearly the basis for substrate specificity of a monolignol β-glucosidase, the structure of Os4BGlu18 was determined by X-ray crystallography. Crystals of Os4BGlu18 and its complex with δ-gluconolactone diffracted to 1.7 and 2.1 Å resolution, respectively. Two protein molecules were found in the asymmetric unit of the P212121 space group of their isomorphous crystals. The Os4BGlu18 structure exhibited the typical (β/α)8 TIM barrel of glycoside hydrolase family 1 (GH1), but the four variable loops and two disulfide bonds appeared significantly different from other known structures of GH1 β-glucosidases. Molecular docking studies of the Os4BGlu18 structure with monolignol substrate ligands placed the glycone in a similar position to the δ-gluconolactone in the complex structure and revealed the interactions between protein and ligands. Molecular docking, multiple sequence alignment, and homology modeling identified amino acid residues at the aglycone-binding site involved in substrate specificity for monolignol β-glucosides. Thus, the structural basis of substrate recognition and hydrolysis by monolignol β-glucosidases was elucidated. PubMed: 33471829DOI: 10.1371/journal.pone.0241325 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
