1y9m
From Proteopedia
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'''Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121''' | '''Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121''' | ||
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[[Category: Polikarpov, I.]] | [[Category: Polikarpov, I.]] | ||
[[Category: Rojas, A L.]] | [[Category: Rojas, A L.]] | ||
| - | [[Category: | + | [[Category: Aspergillus awamori]] |
| - | [[Category: | + | [[Category: Crystallographic structure]] |
| - | [[Category: | + | [[Category: Exo-inulinase]] |
| - | [[Category: | + | [[Category: Glycoside hydrolase family 32]] |
| - | [[Category: | + | [[Category: Native structure]] |
| - | [[Category: | + | [[Category: X-ray structure]] |
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Revision as of 13:02, 3 May 2008
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 Page seeded by OCA on Sat May 3 16:02:53 2008
Categories: Aspergillus awamori | Fructan beta-fructosidase | Single protein | Eneyskaya, E V. | Golubev, A M. | Korneeva, O S. | Kulminskaya, A A. | Nagem, R A.P. | Neustroev, K N. | Polikarpov, I. | Rojas, A L. | Crystallographic structure | Exo-inulinase | Glycoside hydrolase family 32 | Native structure | X-ray structure
