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| [[Image:1ayx.gif|left|200px]]
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| {{Structure
| | ==CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS== |
| |PDB= 1ayx |SIZE=350|CAPTION= <scene name='initialview01'>1ayx</scene>, resolution 1.70Å
| | <StructureSection load='1ayx' size='340' side='right'caption='[[1ayx]], [[Resolution|resolution]] 1.70Å' scene=''> |
| |SITE= <scene name='pdbsite=NUL:Enzyme+Active+Site+And+Two+Catalytic+Carboxylates'>NUL</scene>
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
| | <table><tr><td colspan='2'>[[1ayx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomycopsis_fibuligera Saccharomycopsis fibuligera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYX FirstGlance]. <br> |
| |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| |GENE= GLU1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4944 Saccharomycopsis fibuligera])
| | <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> |
| |DOMAIN=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ayx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayx OCA], [https://pdbe.org/1ayx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayx RCSB], [https://www.ebi.ac.uk/pdbsum/1ayx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayx ProSAT]</span></td></tr> |
| |RELATEDENTRY=
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ayx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayx OCA], [http://www.ebi.ac.uk/pdbsum/1ayx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ayx RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/AMYG_SACFI AMYG_SACFI] |
| | == 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/ay/1ayx_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=1ayx ConSurf]. |
| | <div style="clear:both"></div> |
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| '''CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS'''
| | ==See Also== |
| | | *[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| The yeast Saccharomycopsis fibuligera produces a glucoamylase which belongs to sequence family 15 of glycosyl hydrolases. The structure of the non-glycosyl-ated recombinant enzyme has been determined by molecular replacement and refined against 1.7 A resolution synchrotron data to an R factor of 14.6%. This is the first report of the three-dimensional structure of a yeast family 15 glucoamylase. The refinement from the initial molecular-replacement model was not straightforward. It involved the use of an unrestrained automated refinement procedure (uARP) in combination with the maximum-likelihood refinement program REFMAC. The enzyme consists of 492 amino-acid residues and has 14 alpha-helices, 12 of which form an (alpha/alpha)6 barrel. It contains a single catalytic domain but no starch-binding domain. The fold of the molecule and the active site are compared to the known structure of the catalytic domain of a fungal family 15 glucoamylase and are shown to be closely similar. The active- and specificity-site residues are especially highly conserved. The model of the acarbose inhibitor from the analysis of the fungal enzyme fits tightly into the present structure. The active-site topology is a pocket and hydrolysis proceeds with inversion of the configuration at the anomeric carbon. The enzyme acts as an exo-glycosyl hydrolase. There is a Tris [2-amino-2-(hydroxymethyl)-1,3-propanediol] molecule acting as an inhibitor in the active-site pocket.
| | [[Category: Large Structures]] |
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| ==About this Structure==
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| 1AYX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomycopsis_fibuligera Saccharomycopsis fibuligera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYX OCA].
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| ==Reference==
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| Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7 A resolution., Sevcik J, Solovicova A, Hostinova E, Gasperik J, Wilson KS, Dauter Z, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):854-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9757101 9757101]
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| [[Category: Glucan 1,4-alpha-glucosidase]] | |
| [[Category: Saccharomycopsis fibuligera]] | | [[Category: Saccharomycopsis fibuligera]] |
| [[Category: Single protein]]
| | [[Category: Dauter Z]] |
| [[Category: Dauter, Z.]] | | [[Category: Gasperik J]] |
| [[Category: Gasperik, J.]] | | [[Category: Hostinova E]] |
| [[Category: Hostinova, E.]] | | [[Category: Sevcik J]] |
| [[Category: Sevcik, J.]] | | [[Category: Solovicova A]] |
| [[Category: Solovicova, A.]] | | [[Category: Wilson KS]] |
| [[Category: Wilson, K S.]] | |
| [[Category: glucoamylase]]
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| [[Category: glycosidase]]
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| [[Category: hydrolase]]
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| [[Category: polysaccharide degradation]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:50:12 2008''
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