1y9m
From Proteopedia
(New page: 200px<br /><applet load="1y9m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y9m, resolution 1.89Å" /> '''Crystal structure of...) |
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| - | [[Image:1y9m.jpg|left|200px]]<br /><applet load="1y9m" size=" | + | [[Image:1y9m.jpg|left|200px]]<br /><applet load="1y9m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y9m, resolution 1.89Å" /> | caption="1y9m, resolution 1.89Å" /> | ||
'''Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121'''<br /> | '''Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Exo-inulinases hydrolyze terminal, non-reducing 2,1-linked and 2,6-linked | + | 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== | ==About this Structure== | ||
| - | 1Y9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori] with MAN, NAG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1Y9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fructan beta-fructosidase]] | [[Category: Fructan beta-fructosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Eneyskaya, E | + | [[Category: Eneyskaya, E V.]] |
| - | [[Category: Golubev, A | + | [[Category: Golubev, A M.]] |
| - | [[Category: Korneeva, O | + | [[Category: Korneeva, O S.]] |
| - | [[Category: Kulminskaya, A | + | [[Category: Kulminskaya, A A.]] |
| - | [[Category: Nagem, R | + | [[Category: Nagem, R A.P.]] |
| - | [[Category: Neustroev, K | + | [[Category: Neustroev, K N.]] |
[[Category: Polikarpov, I.]] | [[Category: Polikarpov, I.]] | ||
| - | [[Category: Rojas, A | + | [[Category: Rojas, A L.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: MAN]] | [[Category: MAN]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:07 2008'' |
Revision as of 14:03, 21 February 2008
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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 with , and as ligands. Active as Fructan beta-fructosidase, with EC number 3.2.1.80 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 Thu Feb 21 16:03:07 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. | GOL | MAN | NAG | Crystallographic structure | Exo-inulinase | Glycoside hydrolase family 32 | Native structure | X-ray structure
