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| | <StructureSection load='1uas' size='340' side='right'caption='[[1uas]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1uas' size='340' side='right'caption='[[1uas]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uas]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Orysa Orysa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UAS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orysa Orysa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UAS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] </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=1uas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uas OCA], [http://pdbe.org/1uas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uas RCSB], [http://www.ebi.ac.uk/pdbsum/1uas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uas ProSAT]</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=1uas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uas OCA], [https://pdbe.org/1uas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uas RCSB], [https://www.ebi.ac.uk/pdbsum/1uas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uas ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AGAL_ORYSJ AGAL_ORYSJ]] Hydrolyzes melibiose, raffinose and stachyose in the following decreasing order of reactivity: raffinose, melibiose, stachyose.<ref>PMID:12423882</ref> | + | [[https://www.uniprot.org/uniprot/AGAL_ORYSJ AGAL_ORYSJ]] Hydrolyzes melibiose, raffinose and stachyose in the following decreasing order of reactivity: raffinose, melibiose, stachyose.<ref>PMID:12423882</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[AGAL_ORYSJ] Hydrolyzes melibiose, raffinose and stachyose in the following decreasing order of reactivity: raffinose, melibiose, stachyose.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
alpha-Galactosidases catalyze the hydrolysis of alpha-1,6-linked galactosyl residues from galacto-oligosaccharides and polymeric galacto-(gluco)mannans. The crystal structure of rice alpha-galactosidase has been determined at 1.5A resolution using the multiple isomorphous replacement method. The structure consisted of a catalytic domain and a C-terminal domain and was essentially the same as that of alpha-N-acetylgalactosaminidase, which is the same member of glycosyl hydrolase family 27. The catalytic domain had a (beta/alpha)8-barrel structure, and the C-terminal domain was made up of eight beta-strands containing a Greek key motif. The structure was solved as a complex with d-galactose, providing a mode of substrate binding in detail. The d-galactose molecule was found bound in the active site pocket on the C-terminal side of the central beta-barrel of the catalytic domain. The d-galactose molecule consisted of a mixture of two anomers present in a ratio equal to their natural abundance. Structural comparisons of rice alpha-galactosidase with chicken alpha-N-acetylgalactosaminidase provided further understanding of the substrate recognition mechanism in these enzymes.
Crystal structure of rice alpha-galactosidase complexed with D-galactose.,Fujimoto Z, Kaneko S, Momma M, Kobayashi H, Mizuno H J Biol Chem. 2003 May 30;278(22):20313-8. Epub 2003 Mar 25. PMID:12657636[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim WD, Kobayashi O, Kaneko S, Sakakibara Y, Park GG, Kusakabe I, Tanaka H, Kobayashi H. alpha-Galactosidase from cultured rice (Oryza sativa L. var. Nipponbare) cells. Phytochemistry. 2002 Nov;61(6):621-30. PMID:12423882
- ↑ Fujimoto Z, Kaneko S, Momma M, Kobayashi H, Mizuno H. Crystal structure of rice alpha-galactosidase complexed with D-galactose. J Biol Chem. 2003 May 30;278(22):20313-8. Epub 2003 Mar 25. PMID:12657636 doi:10.1074/jbc.M302292200
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