2hpj

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[[Image:2hpj.jpg|left|200px]]<br /><applet load="2hpj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hpj.jpg|left|200px]]
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caption="2hpj, resolution 1.700&Aring;" />
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'''Crystal structure of the PUB domain of mouse PNGase'''<br />
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{{Structure
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|PDB= 2hpj |SIZE=350|CAPTION= <scene name='initialview01'>2hpj</scene>, resolution 1.700&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [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]
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|GENE= Ngly1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''Crystal structure of the PUB domain of mouse PNGase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2HPJ 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2HPJ OCA].
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2HPJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPJ OCA].
==Reference==
==Reference==
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Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation., Zhao G, Zhou X, Wang L, Li G, Schindelin H, Lennarz WJ, Proc Natl Acad Sci U S A. 2007 May 22;104(21):8785-90. Epub 2007 May 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17496150 17496150]
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Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation., Zhao G, Zhou X, Wang L, Li G, Schindelin H, Lennarz WJ, Proc Natl Acad Sci U S A. 2007 May 22;104(21):8785-90. Epub 2007 May 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17496150 17496150]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]]
[[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]]
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[[Category: winged helix]]
[[Category: winged helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:53 2008''

Revision as of 15:19, 20 March 2008


PDB ID 2hpj

Drag the structure with the mouse to rotate
, resolution 1.700Å
Ligands:
Gene: Ngly1 (Mus musculus)
Activity: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, with EC number 3.5.1.52
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the PUB domain of mouse PNGase


Overview

During endoplasmic reticulum-associated degradation, the multifunctional AAA ATPase p97 is part of a protein degradation complex. p97 associates via its N-terminal domain with various cofactors to recruit ubiquitinated substrates. It also interacts with alternative substrate-processing cofactors, such as Ufd2, Ufd3, and peptide:N-glycanase (PNGase) in higher eukaryotes. These cofactors determine different fates of the substrates and they all bind outside of the N-terminal domain of p97. Here, we describe a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus, which is both necessary and sufficient to mediate interactions of p97 with PNGase and Ufd3. The crystal structure of the N-terminal domain of PNGase in complex with this motif provides detailed insight into the interaction between p97 and its substrate-processing cofactors. Phosphorylation of p97's highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors.

About this Structure

2HPJ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation., Zhao G, Zhou X, Wang L, Li G, Schindelin H, Lennarz WJ, Proc Natl Acad Sci U S A. 2007 May 22;104(21):8785-90. Epub 2007 May 11. PMID:17496150

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