1ayx: Difference between revisions

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<StructureSection load='1ayx' size='340' side='right'caption='[[1ayx]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1ayx' size='340' side='right'caption='[[1ayx]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ayx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_36309 Atcc 36309]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1AYX FirstGlance]. <br>
<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>
</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>
</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLU1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4944 ATCC 36309])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ayx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayx OCA], [http://pdbe.org/1ayx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ayx RCSB], [http://www.ebi.ac.uk/pdbsum/1ayx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYG_SACFI AMYG_SACFI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:9757101<ref>PMID:9757101</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ayx" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 36309]]
[[Category: Glucan 1,4-alpha-glucosidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dauter, Z]]
[[Category: Saccharomycopsis fibuligera]]
[[Category: Gasperik, J]]
[[Category: Dauter Z]]
[[Category: Hostinova, E]]
[[Category: Gasperik J]]
[[Category: Sevcik, J]]
[[Category: Hostinova E]]
[[Category: Solovicova, A]]
[[Category: Sevcik J]]
[[Category: Wilson, K S]]
[[Category: Solovicova A]]
[[Category: Glucoamylase]]
[[Category: Wilson KS]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Polysaccharide degradation]]
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