|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4qll' size='340' side='right'caption='[[4qll]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='4qll' size='340' side='right'caption='[[4qll]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QLL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qll]] 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=4QLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QLL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTT:BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSE'>CTT</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rgl|2rgl]], [[3f5i|3f5i]], [[3scn|3scn]], [[3sct|3sct]], [[3scw|3scw]], [[4qlj|4qlj]], [[4qlk|4qlk]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BGLU1, BGLU7, LOC_Os03g49600, Os03g0703000, Os3BGlu7, OSJNBa0004L11.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qll OCA], [https://pdbe.org/4qll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qll RCSB], [https://www.ebi.ac.uk/pdbsum/4qll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qll ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qll OCA], [http://pdbe.org/4qll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qll RCSB], [http://www.ebi.ac.uk/pdbsum/4qll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qll ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BGL07_ORYSJ BGL07_ORYSJ]] Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.<ref>PMID:14692878</ref> <ref>PMID:19766588</ref> <ref>PMID:18308333</ref> | + | [https://www.uniprot.org/uniprot/BGL07_ORYSJ BGL07_ORYSJ] Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.<ref>PMID:14692878</ref> <ref>PMID:19766588</ref> <ref>PMID:18308333</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-glucosidase]] | |
| - | [[Category: Japanese rice]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cairns, J R.Ketudat]] | + | [[Category: Oryza sativa Japonica Group]] |
| - | [[Category: Pengthaisong, S]] | + | [[Category: Ketudat Cairns JR]] |
| - | [[Category: Beta-alpha-barrel]] | + | [[Category: Pengthaisong S]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Oligosaccharide binding]]
| + | |
| - | [[Category: Transglucosylation]]
| + | |
| Structural highlights
4qll is a 2 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.85Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
BGL07_ORYSJ Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.[1] [2] [3]
Publication Abstract from PubMed
Rice BGlu1 (Os3BGlu7) is a glycoside hydrolase family 1 beta-glucosidase that hydrolyzes cellooligosaccharides with increasing efficiency as the degree of polymerization (DP) increases from 2 to 6, indicating six subsites for glucosyl residue binding. Five subsites have been identified in X-ray crystal structures of cellooligosaccharide complexes with its E176Q acid-base and E386G nucleophile mutants. X-ray crystal structures indicate that cellotetraose binds in a similar mode in BGlu1 E176Q and E386G, but in a different mode in the BGlu1 E386G/Y341A variant, in which glucosyl residue 4 (Glc4) interacts with Q187 instead of the eliminated phenolic group of Y341. Here, we found that the Q187A mutation has little effect on BGlu1 cellooligosaccharide hydrolysis activity or oligosaccharide binding in BGlu1 E176Q, and only slight effects on BGlu1 E386G glycosynthase activity. X-ray crystal structures showed that cellotetraose binds in a different position in BGlu1 E176Q/Y341A, in which it interacts directly with R178 and W337, and the Q187A mutation had little effect on cellotetraose binding. Mutations of R178 and W337 to A had significant and nonadditive effects on oligosaccharide hydrolysis by BGlu1, pNPGlc cleavage and cellooligosaccharide inhibition of BGlu1 E176Q and BGlu1 E386G glycosynthase activity. Hydrolysis activity was partially rescued by Y341 for longer substrates, suggesting stacking of Glc4 on Y341 stabilizes binding of cellooligosaccharides in the optimal position for hydrolysis. This analysis indicates that complex interactions between active site cleft residues modulate substrate binding and hydrolysis.
Effects of active site cleft residues on oligosaccharide binding, hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants.,Pengthaisong S, Ketudat Cairns JR Protein Sci. 2014 Dec;23(12):1738-52. doi: 10.1002/pro.2556. Epub 2014 Oct 23. PMID:25252199[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Opassiri R, Hua Y, Wara-Aswapati O, Akiyama T, Svasti J, Esen A, Ketudat Cairns JR. Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu1. Biochem J. 2004 Apr 1;379(Pt 1):125-31. PMID:14692878 doi:http://dx.doi.org/10.1042/BJ20031485
- ↑ Kuntothom T, Luang S, Harvey AJ, Fincher GB, Opassiri R, Hrmova M, Ketudat Cairns JR. Rice family GH1 glycoside hydrolases with beta-D-glucosidase and beta-D-mannosidase activities. Arch Biochem Biophys. 2009 Nov;491(1-2):85-95. doi: 10.1016/j.abb.2009.09.004., Epub 2009 Sep 18. PMID:19766588 doi:http://dx.doi.org/10.1016/j.abb.2009.09.004
- ↑ Chuenchor W, Pengthaisong S, Robinson RC, Yuvaniyama J, Oonanant W, Bevan DR, Esen A, Chen CJ, Opassiri R, Svasti J, Cairns JR. Structural insights into rice BGlu1 beta-glucosidase oligosaccharide hydrolysis and transglycosylation. J Mol Biol. 2008 Apr 4;377(4):1200-15. Epub 2008 Feb 4. PMID:18308333 doi:10.1016/j.jmb.2008.01.076
- ↑ Pengthaisong S, Ketudat Cairns JR. Effects of active site cleft residues on oligosaccharide binding, hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants. Protein Sci. 2014 Dec;23(12):1738-52. doi: 10.1002/pro.2556. Epub 2014 Oct 23. PMID:25252199 doi:http://dx.doi.org/10.1002/pro.2556
|
