1x9d

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spinqualitylabelsall models PDB ID 1x9d Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1x9d, resolution 1.41Å ()
Ligands:	, , ,
Gene:	MAN1B1 (Homo sapiens)
Activity:	Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113
Related:	1fmi
Structural annotation: Resources: CATH : 1X9Da00 InterPro : Ipr001382 Pfam : PF01532 UniProt : Q9UKM7
Functional annotation: Cellular component: membrane endoplasmic reticulum integral to membrane membrane fraction Biological process: oligosaccharide metabolic process protein amino acid N-linked glycosylation metabolic process Molecular function: hydrolase activity hydrolase activity, acting on glycosyl bonds calcium ion binding mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue 2 Disease 3 Function 4 About this Structure 5 See Also 6 Reference

Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue

Template:ABSTRACT PUBMED 15713668

Disease

[MA1B1_HUMAN] Defects in MAN1B1 are the cause of mental retardation autosomal recessive type 15 (MRT15) [MIM:614202]. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period.^[1]

Function

[MA1B1_HUMAN] Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2).^[2][3]

About this Structure

1x9d is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Mannosidase
• Molecular Playground/ERMan1

Reference

• Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW. Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J Biol Chem. 2005 Apr 22;280(16):16197-207. Epub 2005 Feb 15. PMID:15713668 doi:10.1074/jbc.M500119200

1. ↑ Rafiq MA, Kuss AW, Puettmann L, Noor A, Ramiah A, Ali G, Hu H, Kerio NA, Xiang Y, Garshasbi M, Khan MA, Ishak GE, Weksberg R, Ullmann R, Tzschach A, Kahrizi K, Mahmood K, Naeem F, Ayub M, Moremen KW, Vincent JB, Ropers HH, Ansar M, Najmabadi H. Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability. Am J Hum Genet. 2011 Jul 15;89(1):176-82. doi: 10.1016/j.ajhg.2011.06.006. PMID:21763484 doi:10.1016/j.ajhg.2011.06.006
2. ↑ Herscovics A, Romero PA, Tremblay LO. The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported. Glycobiology. 2002 Apr;12(4):14G-15G. PMID:12090241
3. ↑ Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ. Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol Biol Cell. 2008 Jan;19(1):216-25. Epub 2007 Nov 14. PMID:18003979 doi:10.1091/mbc.E07-05-0505