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PDBsum entry 1mvv

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Hydrolase PDB id
1mvv
Jmol
Contents
Protein chain
313 a.a.
Ligands
M6P ×558
M6P-M6P ×10

References listed in PDB file
Key reference
Title Role of n-Linked oligosaccharide flexibility in mannose phosphorylation of lysosomal enzyme cathepsin l.
Authors J.B.Warner, C.Thalhauser, K.Tao, G.G.Sahagian.
Ref. J Biol Chem, 2002, 277, 41897-41905. [DOI no: 10.1074/jbc.M203097200]
PubMed id 12202476
Abstract
Mannose phosphorylation of N-linked oligosaccharides by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a key step in the targeting of lysosomal enzymes in mammalian cells and tissues. The selectivity of this process is determined by lysine-based phosphorylation signals shared by lysosomal enzymes of diverse structure and function. By introducing new glycosylation sites at several locations on the surface of mouse procathepsin L and modeling oligosaccharide conformations for sites that are phosphorylated, it was shown that the inherent flexibility of N-linked oligosaccharides can account for the specificity of the transferase for oligosaccharides at different locations on the protein. By using this approach, the physical relationship between the lysine-based signal and the site of phosphorylation of mannose residues was determined. The analysis also revealed the existence of additional independent lysine-based phosphorylation signals on procathepsin L, which account for the low level of phosphorylation observed when the primary Lys-54/Lys-99 signal is ablated. Mutagenesis of residues that surround Lys-54 and Lys-99 and demonstration of mannose phosphorylation of a glycosylated derivative of green fluorescent protein provide strong evidence that the cathepsin L phosphorylation signal is a simple structure composed of as few as two well placed lysine residues.
Figure 5.
Fig. 5. Location of the new glycosylation sites on cathepsin L. The wild-type glycosylation site (Asn-221) is shown in blue. The glycosylation sites that were added but were not significantly phosphorylated are shown in red. Glycosylation sites that are highly phosphorylated are shown in green. The -carbons of the critical lysines, Lys-54 and Lys-99, are shown in yellow.
Figure 6.
Fig. 6. Modeling of oligosaccharide clouds on cathepsin L. Modeled structures for oligosaccharide clouds of highly phosphorylated cathepsin L constructs are shown along with an overlay and overlap images. The overlap image is a superposition of the six individual structures. The overlap image shows the oligosaccharide region shared by the six individual structures. Oligosaccharide clouds were modeled as described under "Experimental Procedures." The -carbons of critical lysine residues Lys-54 and Lys-99 are displayed in white. WT, wild type.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 41897-41905) copyright 2002.
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