2hpl: Difference between revisions
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[[Image:2hpl.gif|left|200px]] | [[Image:2hpl.gif|left|200px]] | ||
'''Crystal structure of the mouse p97/PNGase complex''' | {{Structure | ||
|PDB= 2hpl |SIZE=350|CAPTION= <scene name='initialview01'>2hpl</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= | |||
|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] | |||
|GENE= Ngly1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''Crystal structure of the mouse p97/PNGase complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HPL is a [ | 2HPL 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=2HPL OCA]. | ||
==Reference== | ==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:[http:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:56 2008'' | ||
Revision as of 15:19, 20 March 2008
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| 2hpl, resolution 1.80Å | |||||||||||||
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| 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 mouse p97/PNGase complex
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
2HPL 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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