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| | {{STRUCTURE_2rgl| PDB=2rgl | SCENE= }} | | {{STRUCTURE_2rgl| PDB=2rgl | SCENE= }} |
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| - | '''Rice BGlu1 beta-glucosidase, a plant exoglucanase/beta-glucosidase'''
| + | ===Rice BGlu1 beta-glucosidase, a plant exoglucanase/beta-glucosidase=== |
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| - | ==Overview==
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| - | The structures of rice BGlu1 beta-glucosidase, a plant beta-glucosidase active in hydrolyzing cell wall-derived oligosaccharides, and its covalent intermediate with 2-deoxy-2-fluoroglucoside have been solved at 2.2 A and 1.55 A resolution, respectively. The structures were similar to the known structures of other glycosyl hydrolase family 1 (GH1) beta-glucosidases, but showed several differences in the loops around the active site, which lead to an open active site with a narrow slot at the bottom, compatible with the hydrolysis of long beta-1,4-linked oligosaccharides. Though this active site structure is somewhat similar to that of the Paenibacillus polymyxa beta-glucosidase B, which hydrolyzes similar oligosaccharides, molecular docking studies indicate that the residues interacting with the substrate beyond the conserved -1 site are completely different, reflecting the independent evolution of plant and microbial GH1 exo-beta-glucanase/beta-glucosidases. The complex with the 2-fluoroglucoside included a glycerol molecule, which appears to be in a position to make a nucleophilic attack on the anomeric carbon in a transglycosylation reaction. The coordination of the hydroxyl groups suggests that sugars are positioned as acceptors for transglycosylation by their interactions with E176, the catalytic acid/base, and Y131, which is conserved in barley BGQ60/beta-II beta-glucosidase, that has oligosaccharide hydrolysis and transglycosylation activity similar to rice BGlu1. As the rice and barley enzymes have different preferences for cellobiose and cellotriose, residues that appeared to interact with docked oligosaccharides were mutated to those of the barley enzyme to see if the relative activities of rice BGlu1 toward these substrates could be changed to those of BGQ60. Although no single residue appeared to be responsible for these differences, I179, N190 and N245 did appear to interact with the substrates.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18308333}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18308333 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18308333}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glycosidase]] | | [[Category: Glycosidase]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:52:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:41:04 2008'' |
Revision as of 01:41, 29 July 2008
Template:STRUCTURE 2rgl
Rice BGlu1 beta-glucosidase, a plant exoglucanase/beta-glucosidase
Template:ABSTRACT PUBMED 18308333
About this Structure
2RGL is a Single protein structure of sequence from Oryza sativa japonica group. Full crystallographic information is available from OCA.
Reference
Structural insights into rice BGlu1 beta-glucosidase oligosaccharide hydrolysis and transglycosylation., Chuenchor W, Pengthaisong S, Robinson RC, Yuvaniyama J, Oonanant W, Bevan DR, Esen A, Chen CJ, Opassiri R, Svasti J, Cairns JR, J Mol Biol. 2008 Apr 4;377(4):1200-15. Epub 2008 Feb 4. PMID:18308333
Page seeded by OCA on Tue Jul 29 04:41:04 2008
