1ayx

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[[Image:1ayx.gif|left|200px]]<br /><applet load="1ayx" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ayx, resolution 1.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS==
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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.
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<StructureSection load='1ayx' size='340' side='right'caption='[[1ayx]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 1.7&#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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYG_SACFI AMYG_SACFI]
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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/ay/1ayx_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=1ayx ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AYX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomycopsis_fibuligera Saccharomycopsis fibuligera] with <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=NUL:Enzyme+Active+Site+And+Two+Catalytic+Carboxylates'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYX OCA].
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9757101 9757101]
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[[Category: Large Structures]]
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[[Category: Glucan 1,4-alpha-glucosidase]]
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[[Category: Saccharomycopsis fibuligera]]
[[Category: Saccharomycopsis fibuligera]]
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[[Category: Single protein]]
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[[Category: Dauter Z]]
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[[Category: Dauter, Z.]]
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[[Category: Gasperik J]]
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[[Category: Gasperik, J.]]
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[[Category: Hostinova E]]
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[[Category: Hostinova, E.]]
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[[Category: Sevcik J]]
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[[Category: Sevcik, J.]]
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[[Category: Solovicova A]]
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[[Category: Solovicova, A.]]
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[[Category: Wilson KS]]
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[[Category: Wilson, K S.]]
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[[Category: TRS]]
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[[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 Thu Feb 21 11:49:46 2008''
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Current revision

CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS

PDB ID 1ayx

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