1dl2
From Proteopedia
(New page: 200px<br /><applet load="1dl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dl2, resolution 1.54Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1dl2.gif|left|200px]]<br /><applet load="1dl2" size=" | + | [[Image:1dl2.gif|left|200px]]<br /><applet load="1dl2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dl2, resolution 1.54Å" /> | caption="1dl2, resolution 1.54Å" /> | ||
'''CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mannose trimming is not only essential for N-glycan maturation in | + | Mannose trimming is not only essential for N-glycan maturation in mammalian cells but also triggers degradation of misfolded glycoproteins. The crystal structure of the class I alpha1, 2-mannosidase that trims Man(9)GlcNAc(2) to Man(8)GlcNAc(2 )isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (alphaalpha)(7)-barrel in which an N-glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion. The observed protein-carbohydrate interactions provide the first insight into the catalytic mechanism and specificity of this eukaryotic enzyme family and may be used to design inhibitors that prevent degradation of misfolded glycoproteins in genetic diseases. |
==About this Structure== | ==About this Structure== | ||
| - | 1DL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAG, CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1DL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DL2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Herscovics, A.]] | [[Category: Herscovics, A.]] | ||
| - | [[Category: Howell, P | + | [[Category: Howell, P L.]] |
[[Category: Lipari, F.]] | [[Category: Lipari, F.]] | ||
[[Category: Vallee, F.]] | [[Category: Vallee, F.]] | ||
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[[Category: alpha-alpha helix barrel]] | [[Category: alpha-alpha helix barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:43 2008'' |
Revision as of 10:17, 21 February 2008
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CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION
Overview
Mannose trimming is not only essential for N-glycan maturation in mammalian cells but also triggers degradation of misfolded glycoproteins. The crystal structure of the class I alpha1, 2-mannosidase that trims Man(9)GlcNAc(2) to Man(8)GlcNAc(2 )isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (alphaalpha)(7)-barrel in which an N-glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion. The observed protein-carbohydrate interactions provide the first insight into the catalytic mechanism and specificity of this eukaryotic enzyme family and may be used to design inhibitors that prevent degradation of misfolded glycoproteins in genetic diseases.
About this Structure
1DL2 is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 Full crystallographic information is available from OCA.
Reference
Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control., Vallee F, Lipari F, Yip P, Sleno B, Herscovics A, Howell PL, EMBO J. 2000 Feb 15;19(4):581-8. PMID:10675327
Page seeded by OCA on Thu Feb 21 12:17:43 2008
