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1y4w

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|PDB= 1y4w |SIZE=350|CAPTION= <scene name='initialview01'>1y4w</scene>, resolution 1.55&Aring;
|PDB= 1y4w |SIZE=350|CAPTION= <scene name='initialview01'>1y4w</scene>, resolution 1.55&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4w OCA], [http://www.ebi.ac.uk/pdbsum/1y4w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y4w RCSB]</span>
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[[Category: Polikarpov, I.]]
[[Category: Polikarpov, I.]]
[[Category: Rojas, A L.]]
[[Category: Rojas, A L.]]
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[[Category: GOL]]
 
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[[Category: NAG]]
 
[[Category: aspergillus awamori]]
[[Category: aspergillus awamori]]
[[Category: crystallographic structure]]
[[Category: crystallographic structure]]
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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 Mar 20 15:18:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:58:51 2008''

Revision as of 21:58, 30 March 2008


PDB ID 1y4w

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands: ,
Activity: Fructan beta-fructosidase, with EC number 3.2.1.80
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21


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

1Y4W 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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