Source:http://linkedlifedata.com/resource/pubmed/id/15522299
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2004-11-3
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| pubmed:abstractText |
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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/inulinase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0022-2836
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
19
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| pubmed:volume |
344
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
471-80
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15522299-Amino Acid Motifs,
pubmed-meshheading:15522299-Amino Acid Sequence,
pubmed-meshheading:15522299-Aspartic Acid,
pubmed-meshheading:15522299-Aspergillus,
pubmed-meshheading:15522299-Catalytic Domain,
pubmed-meshheading:15522299-Conserved Sequence,
pubmed-meshheading:15522299-Crystallography, X-Ray,
pubmed-meshheading:15522299-Fructose,
pubmed-meshheading:15522299-Glutamine,
pubmed-meshheading:15522299-Glycoside Hydrolases,
pubmed-meshheading:15522299-Glycosylation,
pubmed-meshheading:15522299-Hydrogen Bonding,
pubmed-meshheading:15522299-Models, Molecular,
pubmed-meshheading:15522299-Molecular Sequence Data,
pubmed-meshheading:15522299-Oligosaccharides,
pubmed-meshheading:15522299-Protein Folding,
pubmed-meshheading:15522299-Protein Structure, Secondary,
pubmed-meshheading:15522299-Protein Structure, Tertiary,
pubmed-meshheading:15522299-Sequence Homology, Amino Acid,
pubmed-meshheading:15522299-Substrate Specificity,
pubmed-meshheading:15522299-Water
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| pubmed:year |
2004
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| pubmed:articleTitle |
Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition.
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| pubmed:affiliation |
Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador São-carlense 400, CEP 13560-970, São Carlos, SP, Brazil.
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| pubmed:publicationType |
Journal Article
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