2hpj
From Proteopedia
(New page: 200px<br /><applet load="2hpj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hpj, resolution 1.700Å" /> '''Crystal structure o...) |
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| - | [[Image:2hpj.jpg|left|200px]]<br /><applet load="2hpj" size=" | + | [[Image:2hpj.jpg|left|200px]]<br /><applet load="2hpj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hpj, resolution 1.700Å" /> | caption="2hpj, resolution 1.700Å" /> | ||
'''Crystal structure of the PUB domain of mouse PNGase'''<br /> | '''Crystal structure of the PUB domain of mouse PNGase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 GOL 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: winged helix]] | [[Category: winged helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:06:33 2008'' |
Revision as of 13:06, 23 January 2008
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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 with as ligand. 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.
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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