Structural analysis of rice Os4BGlu18 monolignol [beta]-glucosidase

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From: PLoS ONE(Vol. 16, Issue 1)
Publisher: Public Library of Science
Document Type: Report
Length: 6,875 words
Lexile Measure: 1530L

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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 [beta]-glucosidases. Rice Os4BGlu18 [beta]-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 [beta]-glucosidase, the structure of Os4BGlu18 was determined by X-ray crystallography. Crystals of Os4BGlu18 and its complex with [delta]-gluconolactone diffracted to 1.7 and 2.1 Å resolution, respectively. Two protein molecules were found in the asymmetric unit of the P2.sub.1 2.sub.1 2.sub.1 space group of their isomorphous crystals. The Os4BGlu18 structure exhibited the typical ([beta]/[alpha]).sub.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 [beta]-glucosidases. Molecular docking studies of the Os4BGlu18 structure with monolignol substrate ligands placed the glycone in a similar position to the [delta]-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 [beta]-glucosides. Thus, the structural basis of substrate recognition and hydrolysis by monolignol [beta]-glucosidases was elucidated.

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Gale Document Number: GALE|A649173868