1hcu
From Proteopedia
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| - | [[Image:1hcu.gif|left|200px]] | + | [[Image:1hcu.gif|left|200px]] |
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| - | '''ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI''' | + | {{Structure |
| + | |PDB= 1hcu |SIZE=350|CAPTION= <scene name='initialview01'>1hcu</scene>, resolution 2.37Å | ||
| + | |SITE= <scene name='pdbsite=CAA:Ca+Binding+Site+For+Chain+D'>CAA</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,2-alpha-mannosidase Mannosyl-oligosaccharide 1,2-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.113 3.2.1.113] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HCU is a [ | + | 1HCU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11545593 11545593] |
[[Category: Hypocrea jecorina]] | [[Category: Hypocrea jecorina]] | ||
[[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | [[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | ||
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[[Category: glycosylation]] | [[Category: glycosylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:24 2008'' |
Revision as of 09:35, 20 March 2008
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| , resolution 2.37Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI
Overview
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.
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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