1y4w: Difference between revisions

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[[Image:1y4w.jpg|left|200px]]
{{Seed}}
[[Image:1y4w.png|left|200px]]


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{{STRUCTURE_1y4w|  PDB=1y4w  |  SCENE=  }}  
{{STRUCTURE_1y4w|  PDB=1y4w  |  SCENE=  }}  


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




==Overview==
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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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{{ABSTRACT_PUBMED_15522299}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15522299 15522299]
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]
Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori., Arand M, Golubev AM, Neto JR, Polikarpov I, Wattiez R, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Shabalin KA, Shishliannikov SM, Chepurnaya OV, Neustroev KN, Biochem J. 2002 Feb 15;362(Pt 1):131-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11829749 11829749]
[[Category: Aspergillus awamori]]
[[Category: Aspergillus awamori]]
[[Category: Fructan beta-fructosidase]]
[[Category: Fructan beta-fructosidase]]
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[[Category: Native structure]]
[[Category: Native structure]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
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