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2z8g

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{{STRUCTURE_2z8g| PDB=2z8g | SCENE= }}
{{STRUCTURE_2z8g| PDB=2z8g | SCENE= }}
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'''Aspergillus niger ATCC9642 isopullulanase complexed with isopanose'''
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===Aspergillus niger ATCC9642 isopullulanase complexed with isopanose===
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==Overview==
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An isopullulanase (IPU) from Aspergillus niger ATCC9642 hydrolyzes alpha-1,4-glucosidic linkages of pullulan to produce isopanose. Although IPU does not hydrolyze dextran, it is classified into glycoside hydrolase family 49 (GH49), major members of which are dextran-hydrolyzing enzymes. IPU is highly glycosylated, making it difficult to obtain its crystal. We used endoglycosidase H(f) to cleave the N-linked oligosaccharides of IPU, and we here determined the unliganded and isopanose-complexed forms of IPU, both solved at 1.7-A resolution. IPU is composed of domains N and C joined by a short linker, with electron density maps for 11 or 12 N-acetylglucosamine residues per molecule. Domain N consists of 13 beta-strands and forms a beta-sandwich. Domain C, where the active site is located, forms a right-handed beta-helix, and the lengths of the pitches of each coil of the beta-helix are similar to those of GH49 dextranase and GH28 polygalacturonase. The entire structure of IPU resembles that of a GH49 enzyme, Penicillium minioluteum dextranase (Dex49A), despite a difference in substrate specificity. Compared with the active sites of IPU and Dex49A, the amino acid residues participating in subsites +2 and +3 are not conserved, and the glucose residues of isopanose bound to IPU completely differ in orientation from the corresponding glucose residues of isomaltose bound to Dex49A. The shape of the catalytic cleft characterized by the seventh coil of the beta-helix and a loop from domain N appears to be critical in determining the specificity of IPU for pullulan.
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{{ABSTRACT_PUBMED_18155243}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49., Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T, J Mol Biol. 2008 Feb 8;376(1):210-20. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18155243 18155243]
Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49., Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T, J Mol Biol. 2008 Feb 8;376(1):210-20. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18155243 18155243]
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Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase., Akeboshi H, Tonozuka T, Furukawa T, Ichikawa K, Aoki H, Shimonishi A, Nishikawa A, Sakano Y, Eur J Biochem. 2004 Nov;271(22):4420-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15560783 15560783]
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Construction of an efficient expression system for Aspergillus isopullulanase in Pichia pastoris, and a simple purification method., Akeboshi H, Kashiwagi Y, Aoki H, Tonozuka T, Nishikawa A, Sakano Y, Biosci Biotechnol Biochem. 2003 May;67(5):1149-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12834298 12834298]
[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
[[Category: Isopullulanase]]
[[Category: Isopullulanase]]
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[[Category: Pullulan]]
[[Category: Pullulan]]
[[Category: Secreted]]
[[Category: Secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:19:50 2008''

Revision as of 16:19, 28 July 2008

Image:2z8g.png

Template:STRUCTURE 2z8g

Aspergillus niger ATCC9642 isopullulanase complexed with isopanose

Template:ABSTRACT PUBMED 18155243

About this Structure

2Z8G is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49., Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T, J Mol Biol. 2008 Feb 8;376(1):210-20. Epub 2007 Dec 5. PMID:18155243

Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase., Akeboshi H, Tonozuka T, Furukawa T, Ichikawa K, Aoki H, Shimonishi A, Nishikawa A, Sakano Y, Eur J Biochem. 2004 Nov;271(22):4420-7. PMID:15560783

Construction of an efficient expression system for Aspergillus isopullulanase in Pichia pastoris, and a simple purification method., Akeboshi H, Kashiwagi Y, Aoki H, Tonozuka T, Nishikawa A, Sakano Y, Biosci Biotechnol Biochem. 2003 May;67(5):1149-53. PMID:12834298

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