1xsj
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1xsj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xsj, resolution 2.10Å" /> '''Structure of a Famil...) |
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| - | [[Image:1xsj.gif|left|200px]]<br /><applet load="1xsj" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1xsj, resolution 2.10Å" /> | ||
| - | '''Structure of a Family 31 alpha glycosidase'''<br /> | ||
| - | == | + | ==Structure of a Family 31 alpha glycosidase== |
| - | We have determined the first structure of a family 31 alpha-glycosidase, that of YicI from Escherichia coli, both free and trapped as a | + | <StructureSection load='1xsj' size='340' side='right'caption='[[1xsj]], [[Resolution|resolution]] 2.10Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1xsj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=1xsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsj OCA], [https://pdbe.org/1xsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsj RCSB], [https://www.ebi.ac.uk/pdbsum/1xsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/XYLS_ECOLI XYLS_ECOLI] Can catalyze the transfer of alpha-xylosyl residue from alpha-xyloside to xylose, glucose, mannose, fructose, maltose, isomaltose, nigerose, kojibiose, sucrose and trehalose.<ref>PMID:15294295</ref> <ref>PMID:15501829</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xs/1xsj_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1xsj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have determined the first structure of a family 31 alpha-glycosidase, that of YicI from Escherichia coli, both free and trapped as a 5-fluoroxylopyranosyl-enzyme intermediate via reaction with 5-fluoro-alpha-D-xylopyranosyl fluoride. Our 2.2-A resolution structure shows an intimately associated hexamer with structural elements from several monomers converging at each of the six active sites. Our kinetic and mass spectrometry analyses verified several of the features observed in our structural data, including a covalent linkage from the carboxylate side chain of the identified nucleophile Asp(416) to C-1 of the sugar ring. Structure-based sequence comparison of YicI with the mammalian alpha-glucosidases lysosomal alpha-glucosidase and sucrase-isomaltase predicts a high level of structural similarity and provides a foundation for understanding the various mutations of these enzymes that elicit human disease. | ||
| - | + | Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate.,Lovering AL, Lee SS, Kim YW, Withers SG, Strynadka NC J Biol Chem. 2005 Jan 21;280(3):2105-15. Epub 2004 Oct 22. PMID:15501829<ref>PMID:15501829</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1xsj" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Xylosidase 3D structures|Xylosidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim YW]] | ||
| + | [[Category: Lee SS]] | ||
| + | [[Category: Lovering AL]] | ||
| + | [[Category: Strynadka NC]] | ||
| + | [[Category: Withers SG]] | ||
Current revision
Structure of a Family 31 alpha glycosidase
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