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1uas

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(New page: 200px<br /><applet load="1uas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uas, resolution 1.50&Aring;" /> '''Crystal structure of...)
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[[Image:1uas.jpg|left|200px]]<br /><applet load="1uas" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uas, resolution 1.50&Aring;" />
 
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'''Crystal structure of rice alpha-galactosidase'''<br />
 
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==Overview==
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==Crystal structure of rice alpha-galactosidase==
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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.
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<StructureSection load='1uas' size='340' side='right'caption='[[1uas]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. 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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ua/1uas_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uas ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:12657636</ref>
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1UAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with GLA, SO4, PT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UAS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12657636 12657636]
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</div>
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[[Category: Alpha-galactosidase]]
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<div class="pdbe-citations 1uas" style="background-color:#fffaf0;"></div>
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[[Category: Oryza sativa]]
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[[Category: Single protein]]
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[[Category: Fujimoto, Z.]]
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[[Category: Kaneko, S.]]
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[[Category: Kobayashi, H.]]
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[[Category: Mizuno, H.]]
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[[Category: Momma, M.]]
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[[Category: GLA]]
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[[Category: GOL]]
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[[Category: PT]]
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[[Category: SO4]]
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[[Category: beta-alpha-barrel]]
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[[Category: greek key motif]]
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[[Category: tim-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:58:09 2007''
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==See Also==
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*[[Galactosidase 3D structures|Galactosidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Oryza sativa]]
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[[Category: Fujimoto Z]]
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[[Category: Kaneko S]]
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[[Category: Kobayashi H]]
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[[Category: Mizuno H]]
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[[Category: Momma M]]

Current revision

Crystal structure of rice alpha-galactosidase

PDB ID 1uas

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