1nxc
From Proteopedia
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| - | [[Image:1nxc.jpg|left|200px]] | + | [[Image:1nxc.jpg|left|200px]] |
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| - | '''Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)''' | + | {{Structure |
| + | |PDB= 1nxc |SIZE=350|CAPTION= <scene name='initialview01'>1nxc</scene>, resolution 1.51Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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= man1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NXC is a [ | + | 1NXC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXC OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases., Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW, J Biol Chem. 2004 Jul 9;279(28):29774-86. Epub 2004 Apr 21. PMID:[http:// | + | Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases., Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW, J Biol Chem. 2004 Jul 9;279(28):29774-86. Epub 2004 Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15102839 15102839] |
[[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | [[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: psi]] | [[Category: psi]] | ||
[[Category: secsg]] | [[Category: secsg]] | ||
| - | [[Category: southeast collaboratory for structural | + | [[Category: southeast collaboratory for structural genomic]] |
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''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 13:02:55 2008'' |
Revision as of 11:02, 20 March 2008
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| , resolution 1.51Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | man1a (Mus musculus) | ||||||
| Activity: | Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)
Overview
Three subfamilies of mammalian Class 1 processing alpha1,2-mannosidases (family 47 glycosidases) play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum (ER) and Golgi complex as well as influencing the timing and recognition for disposal of terminally unfolded proteins by ER-associated degradation. In an effort to define the structural basis for substrate recognition among Class 1 mannosidases, we have crystallized murine Golgi mannosidase IA (space group P2(1)2(1)2(1)), and the structure was solved to 1.5-A resolution by molecular replacement. The enzyme assumes an (alphaalpha)(7) barrel structure with a Ca(2+) ion coordinated at the base of the barrel similar to other Class 1 mannosidases. Critical residues within the barrel structure that coordinate the Ca(2+) ion or presumably bind and catalyze the hydrolysis of the glycone are also highly conserved. A Man(6)GlcNAc(2) oligosaccharide attached to Asn(515) in the murine enzyme was found to extend into the active site of an adjoining protein unit in the crystal lattice in a presumed enzyme-product complex. In contrast to an analogous complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes a different conformation to present an alternate oligosaccharide branch into the active site pocket. A comparison of the observed protein-carbohydrate interactions for the murine Golgi enzyme with the binding cleft topologies of the other family 47 glycosidases provides a framework for understanding the structural basis for substrate recognition among this class of enzymes.
About this Structure
1NXC is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases., Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW, J Biol Chem. 2004 Jul 9;279(28):29774-86. Epub 2004 Apr 21. PMID:15102839
Page seeded by OCA on Thu Mar 20 13:02:55 2008
Categories: Mannosyl-oligosaccharide 1,2-alpha-mannosidase | Mus musculus | Single protein | Karaveg, K. | Liu, Z J. | Moremen, K W. | Rose, J. | SECSG, Southeast Collaboratory for Structural Genomics. | Tempel, W. | Wang, B C. | CA | MAN | Glycosidase | Mannosidase | Protein structure initiative | Psi | Secsg | Southeast collaboratory for structural genomic | Structural genomic
