1hcu

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[[Image:1hcu.gif|left|200px]]
[[Image:1hcu.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1hcu |SIZE=350|CAPTION= <scene name='initialview01'>1hcu</scene>, resolution 2.37&Aring;
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The line below this paragraph, containing "STRUCTURE_1hcu", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAA:Ca+Binding+Site+For+Chain+D'>CAA</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1hcu| PDB=1hcu | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcu OCA], [http://www.ebi.ac.uk/pdbsum/1hcu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hcu RCSB]</span>
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}}
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'''ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI'''
'''ALPHA-1,2-MANNOSIDASE FROM TRICHODERMA REESEI'''
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[[Category: Contreras, R.]]
[[Category: Contreras, R.]]
[[Category: Petegem, F Van.]]
[[Category: Petegem, F Van.]]
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[[Category: glycosyl hydrolase]]
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[[Category: Glycosyl hydrolase]]
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[[Category: glycosylation]]
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[[Category: Glycosylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:42:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:02:28 2008''
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Revision as of 15:42, 2 May 2008

Template:STRUCTURE 1hcu

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 Page seeded by OCA on Fri May 2 18:42:32 2008

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