7d6b

<table><tr><td colspan='2'>[[7d6b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D6B FirstGlance]. <br>

== Function ==

[https://www.uniprot.org/uniprot/BGL18_ORYSJ BGL18_ORYSJ] Hydrolyzes glycosides and monolignol glucosides (PubMed:25219312). Can hydrolyze para-nitrophenyl beta-D-glucopyranoside (pNPGlc) in vitro (PubMed:23811195, PubMed:25219312). Hydrolyzes para-nitrophenyl beta-D-fucopyranoside, para-nitrophenyl beta-D-galactopyranoside and para-nitrophenyl beta-D-xylopyranoside in vitro (PubMed:25219312). Hydrolyzes the monolignol glucosides coniferin and syringin with high catalytic efficiencies (PubMed:25219312).<ref>PMID:23811195</ref> <ref>PMID:25219312</ref>

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== Publication Abstract from PubMed ==

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 A 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 (beta/alpha)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.

Structural analysis of rice Os4BGlu18 monolignol beta-glucosidase.,Baiya S, Pengthaisong S, Kitjaruwankul S, Ketudat Cairns JR PLoS One. 2021 Jan 20;16(1):e0241325. doi: 10.1371/journal.pone.0241325. , eCollection 2021. PMID:33471829<ref>PMID:33471829</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Oryza sativa Japonica Group]]