1y4w: Difference between revisions
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|PDB= 1y4w |SIZE=350|CAPTION= <scene name='initialview01'>1y4w</scene>, resolution 1.55Å | |PDB= 1y4w |SIZE=350|CAPTION= <scene name='initialview01'>1y4w</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|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] | |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= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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.]] | ||
[[Category: aspergillus awamori]] | [[Category: aspergillus awamori]] | ||
[[Category: crystallographic structure]] | [[Category: crystallographic structure]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''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
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| 1y4w, resolution 1.55Å | |||||||||||||
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| Ligands: | GOL, NAG | ||||||||||||
| 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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