2ri9

Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog

spinqualitylabelsall models 2ri9, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ri9 is a 2 chain structure with sequence from Atcc 1109. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL, LDY, MAN, MMA, NAG, NDG Related: 1kkt, 1kre, 1krf, 2ri8 Gene: MSDC (ATCC 1109) Activity: Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MAN12_PENCI] Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Class I alpha-mannosidases (glycoside hydrolase family GH47) play key roles in the maturation of N-glycans and the ER-associated degradation of unfolded glycoproteins. The 1.95 A resolution structure of a fungal alpha-1,2-mannosidase in complex with the substrate analogue methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside (LM) shows the intact disaccharide spanning the -1/+1 subsites, with the D-lyxoside ring in the -1 subsite in the 1C4 chair conformation, and provides insight into the mechanism of catalysis. The absence of the C5' hydroxymethyl group on the D-lyxoside moiety results in the side chain of Arg407 adopting two alternative conformations: the minor one interacting with Asp375 and the major one interacting with both the D-lyxoside and the catalytic base Glu409, thus disrupting its function. Chemical modification of Asp375 has previously been shown to inactivate the enzyme. Taken together, the data suggest that Arg407, which belongs to the conserved sequence motif RPExxE, may act to modulate the activity of the enzyme. The proposed mechanism for modulating the activity is potentially a general mechanism for this superfamily. Modulation of activity by Arg407: structure of a fungal alpha-1,2-mannosidase in complex with a substrate analogue.,Lobsanov YD, Yoshida T, Desmet T, Nerinckx W, Yip P, Claeyssens M, Herscovics A, Howell PL Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):227-36. Epub 2008, Feb 20. PMID:18323617 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mannosidase 3D structures

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