2f4m

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[[Image:2f4m.gif|left|200px]]
[[Image:2f4m.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2f4m |SIZE=350|CAPTION= <scene name='initialview01'>2f4m</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2f4m", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= Rad23b, Mhr23b ([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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|DOMAIN=
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{{STRUCTURE_2f4m| PDB=2f4m | SCENE= }}
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|RELATEDENTRY=[[2f4o|2F4O]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f4m OCA], [http://www.ebi.ac.uk/pdbsum/2f4m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f4m RCSB]</span>
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}}
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'''The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs'''
'''The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs'''
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Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways., Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H, J Biol Chem. 2006 May 12;281(19):13751-61. Epub 2006 Feb 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16500903 16500903]
Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways., Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H, J Biol Chem. 2006 May 12;281(19):13751-61. Epub 2006 Feb 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16500903 16500903]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]]
 
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Kisker, C.]]
[[Category: Kisker, C.]]
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[[Category: Zhao, G.]]
[[Category: Zhao, G.]]
[[Category: Zhou, X.]]
[[Category: Zhou, X.]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: nucleotide excision repair]]
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[[Category: Nucleotide excision repair]]
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[[Category: peptide:n-glycanase]]
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[[Category: Peptide:n-glycanase]]
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[[Category: transglutaminase]]
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[[Category: Transglutaminase]]
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[[Category: ubiquitin-dependent protein degradation]]
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[[Category: Ubiquitin-dependent protein degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:27:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:57:48 2008''
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Revision as of 00:27, 4 May 2008

Template:STRUCTURE 2f4m

The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs


Overview

Peptide N-glycanase removes N-linked oligosaccharides from misfolded glycoproteins as part of the endoplasmic reticulum-associated degradation pathway. This process involves the formation of a tight complex of peptide N-glycanase with Rad23 in yeast and the orthologous HR23 proteins in mammals. In addition to its function in endoplasmic reticulum-associated degradation, HR23 is also involved in DNA repair, where it plays an important role in damage recognition in complex with the xeroderma pigmentosum group C protein. To characterize the dual role of HR23, we have determined the high resolution crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B. Peptide N-glycanase features a large cleft between its catalytic cysteine protease core and zinc binding domain. Opposite the zinc binding domain is the HR23B-interacting region, and surprisingly, the complex interface is fundamentally different from the orthologous yeast peptide N-glycanase-Rad23 complex. Different regions on both proteins are involved in complex formation, revealing an amazing degree of divergence in the interaction between two highly homologous proteins. Furthermore, the mouse peptide N-glycanase-HR23B complex mimics the interaction between xeroderma pigmentosum group C and HR23B, thereby providing a first structural model of how the two proteins interact within the nucleotide excision repair cascade in higher eukaryotes. The different interaction interfaces of the xeroderma pigmentosum group C binding domains in yeast and mammals suggest a co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.

About this Structure

2F4M is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways., Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H, J Biol Chem. 2006 May 12;281(19):13751-61. Epub 2006 Feb 24. PMID:16500903 Page seeded by OCA on Sun May 4 03:27:12 2008

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