1hcu

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{{STRUCTURE_1hcu| PDB=1hcu | SCENE= }}
{{STRUCTURE_1hcu| PDB=1hcu | SCENE= }}
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'''ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI'''
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===ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI===
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==Overview==
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The process of N-glycosylation of eukaryotic proteins involves a range of host enzymes that delete or add saccharide monomers. While endoplasmic reticulum (E.R.) mannosidases cleave only one mannose to produce the Man8B isomer, an alpha-1,2-mannosidase from Trichoderma reesei can sequentially cleave all four 1,2-linked mannose sugars from a Man(9)GlcNAc(2) oligosaccharide, a feature reminiscent of the activity of Golgi mannosidases. We now report the structure of the T. reesei enzyme at 2.37 A resolution. The enzyme folds as an (alpha alpha)(7) barrel. The substrate-binding site of the T. reesei mannosidase differs appreciably from the Saccharomyces cerevisiae enzyme. In the former, shorter loops at the surface allow substrate protein to come closer to the catalytic site. There is more internal space available, so that different oligosaccharide conformations are sterically allowed in the T. reesei alpha-1,2-mannosidase.
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(as it appears on PubMed at http://www.pubmed.gov), where 11545593 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11545593}}
==About this Structure==
==About this Structure==
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[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosylation]]
[[Category: Glycosylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:00:09 2008''

Revision as of 05:00, 1 July 2008

Template:STRUCTURE 1hcu

ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI

Template:ABSTRACT PUBMED 11545593

About this Structure

1HCU is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

Reference

Trichoderma reesei alpha-1,2-mannosidase: structural basis for the cleavage of four consecutive mannose residues., Van Petegem F, Contreras H, Contreras R, Van Beeumen J, J Mol Biol. 2001 Sep 7;312(1):157-65. PMID:11545593

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