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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[[Image:1ayx.gif|left|200px]]
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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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{{Structure
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|PDB= 1ayx |SIZE=350|CAPTION= <scene name='initialview01'>1ayx</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=NUL:Enzyme+Active+Site+And+Two+Catalytic+Carboxylates'>NUL</scene>
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|LIGAND= <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [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]
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|GENE= GLU1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4944 Saccharomycopsis fibuligera])
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}}
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'''CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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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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].
==Reference==
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9757101 9757101]
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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]
[[Category: Glucan 1,4-alpha-glucosidase]]
[[Category: Glucan 1,4-alpha-glucosidase]]
[[Category: Saccharomycopsis fibuligera]]
[[Category: Saccharomycopsis fibuligera]]
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[[Category: polysaccharide degradation]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:04 2008''

Revision as of 08:04, 20 March 2008


PDB ID 1ayx

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands:
Gene: GLU1 (Saccharomycopsis fibuligera)
Activity: Glucan 1,4-alpha-glucosidase, with EC number 3.2.1.3
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS


Overview

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.

About this Structure

1AYX is a Single protein structure of sequence from Saccharomycopsis fibuligera. Full crystallographic information is available from OCA.

Reference

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

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