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| | <StructureSection load='4bfn' size='340' side='right'caption='[[4bfn]], [[Resolution|resolution]] 1.32Å' scene=''> | | <StructureSection load='4bfn' size='340' side='right'caption='[[4bfn]], [[Resolution|resolution]] 1.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bfn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_56536 Atcc 56536]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BFN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bfn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizopus_arrhizus Rhizopus arrhizus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BFN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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]] 1.32Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bfo|4bfo]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,4-alpha-glucosidase Glucan 1,4-alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.3 3.2.1.3] </span></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=4bfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bfn OCA], [https://pdbe.org/4bfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bfn RCSB], [https://www.ebi.ac.uk/pdbsum/4bfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bfn ProSAT]</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=4bfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bfn OCA], [http://pdbe.org/4bfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bfn RCSB], [http://www.ebi.ac.uk/pdbsum/4bfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bfn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2VC81_RHIOR Q2VC81_RHIOR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 56536]] | |
| - | [[Category: Glucan 1,4-alpha-glucosidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chu, C H]] | + | [[Category: Rhizopus arrhizus]] |
| - | [[Category: Li, K M]] | + | [[Category: Chu CH]] |
| - | [[Category: Lin, S W]] | + | [[Category: Li KM]] |
| - | [[Category: Sun, Y J]] | + | [[Category: Lin SW]] |
| - | [[Category: Carbohydrate binding]] | + | [[Category: Sun YJ]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q2VC81_RHIOR
Publication Abstract from PubMed
Glucoamylases are responsible for hydrolysis of starch and polysaccharides to yield beta-D-glucose. Rhizopus oryzae glucoamylase (RoGA) is composed of an N-terminal starch binding domain (SBD) and a C-terminal catalytic domain connected by an O-glycosylated linker. Two carbohydrate-binding sites in RoSBD have been identified, site I is created by three highly conserved aromatic residues, Trp47, Tyr83, and Tyr94, and site II is built up by Tyr32 and Phe58. Here the two crystal structures of RoSBD in complex with only alpha-(1,6)-linked isomaltotriose (RoSBD-isoG3) and isomaltotetraose (RoSBD-isoG4) have been determined at 1.2 A and 1.3 A, respectively. Interestingly, site II binding is observed in both complexes, while site I binding is only found in the RoSBD-isoG4 complex. Hence, site II acts as the recognition binding site for carbohydrate and site I accommodates site II to bind isoG4. Site I participates in sugar binding only when the number of glucosyl units of oligosaccharides is more than three. Taken together, two carbohydrate binding sites in RoSBD cooperate to reinforce binding mode of glucoamylase with polysaccharides as well as the starch. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.
Crystal Structures of Starch Binding Domain from Rhizopus oryzae Glucoamylase in Complex with Isomaltooligosaccharide: Insights into Polysaccharide Binding Mechanism of CBM21 Family.,Chu CH, Li KM, Lin SW, Chang MD, Jiang TY, Sun YJ Proteins. 2013 Oct 9. doi: 10.1002/prot.24446. PMID:24108499[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chu CH, Li KM, Lin SW, Chang MD, Jiang TY, Sun YJ. Crystal Structures of Starch Binding Domain from Rhizopus oryzae Glucoamylase in Complex with Isomaltooligosaccharide: Insights into Polysaccharide Binding Mechanism of CBM21 Family. Proteins. 2013 Oct 9. doi: 10.1002/prot.24446. PMID:24108499 doi:http://dx.doi.org/10.1002/prot.24446
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