1y9m

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[[Image:1y9m.jpg|left|200px]]<br /><applet load="1y9m" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y9m.jpg|left|200px]]
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caption="1y9m, resolution 1.89&Aring;" />
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'''Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121'''<br />
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{{Structure
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|PDB= 1y9m |SIZE=350|CAPTION= <scene name='initialview01'>1y9m</scene>, resolution 1.89&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Fructan_beta-fructosidase Fructan beta-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.80 3.2.1.80]
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|GENE=
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}}
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'''Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructan_beta-fructosidase Fructan beta-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.80 3.2.1.80] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9M OCA].
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1Y9M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9M OCA].
==Reference==
==Reference==
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Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition., Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I, J Mol Biol. 2004 Nov 19;344(2):471-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15522299 15522299]
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Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition., Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I, J Mol Biol. 2004 Nov 19;344(2):471-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15522299 15522299]
[[Category: Aspergillus awamori]]
[[Category: Aspergillus awamori]]
[[Category: Fructan beta-fructosidase]]
[[Category: Fructan beta-fructosidase]]
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[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:09 2008''

Revision as of 13:20, 20 March 2008

Image:1y9m.jpg


PDB ID 1y9m

Drag the structure with the mouse to rotate
, resolution 1.89Å
Ligands: , and
Activity: Fructan beta-fructosidase, with EC number 3.2.1.80
Coordinates: save as pdb, mmCIF, xml



Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121


Overview

Exo-inulinases hydrolyze terminal, non-reducing 2,1-linked and 2,6-linked beta-d-fructofuranose residues in inulin, levan and sucrose releasing beta-d-fructose. We present the X-ray structure at 1.55A resolution of exo-inulinase from Aspergillus awamori, a member of glycoside hydrolase family 32, solved by single isomorphous replacement with the anomalous scattering method using the heavy-atom sites derived from a quick cryo-soaking technique. The tertiary structure of this enzyme folds into two domains: the N-terminal catalytic domain of an unusual five-bladed beta-propeller fold and the C-terminal domain folded into a beta-sandwich-like structure. Its structural architecture is very similar to that of another member of glycoside hydrolase family 32, invertase (beta-fructosidase) from Thermotoga maritima, determined recently by X-ray crystallography The exo-inulinase is a glycoprotein containing five N-linked oligosaccharides. Two crystal forms obtained under similar crystallization conditions differ by the degree of protein glycosylation. The X-ray structure of the enzyme:fructose complex, at a resolution of 1.87A, reveals two catalytically important residues: Asp41 and Glu241, a nucleophile and a catalytic acid/base, respectively. The distance between the side-chains of these residues is consistent with a double displacement mechanism of reaction. Asp189, which is part of the Arg-Asp-Pro motif, provides hydrogen bonds important for substrate recognition.

About this Structure

1Y9M is a Single protein structure of sequence from Aspergillus awamori. Full crystallographic information is available from OCA.

Reference

Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition., Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I, J Mol Biol. 2004 Nov 19;344(2):471-80. PMID:15522299

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