2i74: Difference between revisions
New page: left|200px<br /><applet load="2i74" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i74, resolution 1.750Å" /> '''Crystal structure o... |
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[[Image:2i74.jpg|left|200px]]<br /><applet load="2i74" size=" | [[Image:2i74.jpg|left|200px]]<br /><applet load="2i74" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2i74, resolution 1.750Å" /> | caption="2i74, resolution 1.750Å" /> | ||
'''Crystal structure of mouse Peptide N-Glycanase C-terminal domain in complex with mannopentaose'''<br /> | '''Crystal structure of mouse Peptide N-Glycanase C-terminal domain in complex with mannopentaose'''<br /> | ||
==Overview== | ==Overview== | ||
The inability of certain N-linked glycoproteins to adopt their native | The inability of certain N-linked glycoproteins to adopt their native conformation in the endoplasmic reticulum (ER) leads to their retrotranslocation into the cytosol and subsequent degradation by the proteasome. In this pathway the cytosolic peptide-N-glycanase (PNGase) cleaves the N-linked glycan chains off denatured glycoproteins. PNGase is highly conserved in eukaryotes and plays an important role in ER-associated protein degradation. In higher eukaryotes, PNGase has an N-terminal and a C-terminal extension in addition to its central catalytic domain, which is structurally and functionally related to transglutaminases. Although the N-terminal domain of PNGase is involved in protein-protein interactions, the function of the C-terminal domain has not previously been characterized. Here, we describe biophysical, biochemical, and crystallographic studies of the mouse PNGase C-terminal domain, including visualization of a complex between this domain and mannopentaose. These studies demonstrate that the C-terminal domain binds to the mannose moieties of N-linked oligosaccharide chains, and we further show that it enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins. | ||
==About this Structure== | ==About this Structure== | ||
2I74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ACT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine_amidase Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.52 3.5.1.52] Full crystallographic information is available from [http:// | 2I74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine_amidase Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.52 3.5.1.52] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I74 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]] | [[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lennarz, W | [[Category: Lennarz, W J.]] | ||
[[Category: Li, G.]] | [[Category: Li, G.]] | ||
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
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[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:49:51 2008'' | ||
Revision as of 18:49, 21 February 2008
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Crystal structure of mouse Peptide N-Glycanase C-terminal domain in complex with mannopentaose
OverviewOverview
The inability of certain N-linked glycoproteins to adopt their native conformation in the endoplasmic reticulum (ER) leads to their retrotranslocation into the cytosol and subsequent degradation by the proteasome. In this pathway the cytosolic peptide-N-glycanase (PNGase) cleaves the N-linked glycan chains off denatured glycoproteins. PNGase is highly conserved in eukaryotes and plays an important role in ER-associated protein degradation. In higher eukaryotes, PNGase has an N-terminal and a C-terminal extension in addition to its central catalytic domain, which is structurally and functionally related to transglutaminases. Although the N-terminal domain of PNGase is involved in protein-protein interactions, the function of the C-terminal domain has not previously been characterized. Here, we describe biophysical, biochemical, and crystallographic studies of the mouse PNGase C-terminal domain, including visualization of a complex between this domain and mannopentaose. These studies demonstrate that the C-terminal domain binds to the mannose moieties of N-linked oligosaccharide chains, and we further show that it enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins.
About this StructureAbout this Structure
2I74 is a Single protein structure of sequence from Mus musculus with and as ligands. Active as Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, with EC number 3.5.1.52 Full crystallographic information is available from OCA.
ReferenceReference
Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module., Zhou X, Zhao G, Truglio JJ, Wang L, Li G, Lennarz WJ, Schindelin H, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17214-9. Epub 2006 Nov 6. PMID:17088551
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