1nxc
From Proteopedia
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|PDB= 1nxc |SIZE=350|CAPTION= <scene name='initialview01'>1nxc</scene>, resolution 1.51Å | |PDB= 1nxc |SIZE=350|CAPTION= <scene name='initialview01'>1nxc</scene>, resolution 1.51Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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] | + | |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> |
|GENE= man1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= man1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01532 Glyco_hydro_47]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxc OCA], [http://www.ebi.ac.uk/pdbsum/1nxc PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1nxc RCSB]</span> | ||
}} | }} | ||
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[[Category: Tempel, W.]] | [[Category: Tempel, W.]] | ||
[[Category: Wang, B C.]] | [[Category: Wang, B C.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MAN]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
[[Category: mannosidase]] | [[Category: mannosidase]] | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:59:19 2008'' |
Revision as of 03:59, 26 March 2008
| |||||||
| , resolution 1.51Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | man1a (Mus musculus) | ||||||
| Activity: | Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 | ||||||
| Domains: | Glyco_hydro_47 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| 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 Wed Mar 26 05:59:19 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. | Glycosidase | Mannosidase | Protein structure initiative | Psi | Secsg | Southeast collaboratory for structural genomic | Structural genomic
