2cm0: Difference between revisions
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[[Image:2cm0.gif|left|200px]] | [[Image:2cm0.gif|left|200px]] | ||
'''THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.''' | {{Structure | ||
|PDB= 2cm0 |SIZE=350|CAPTION= <scene name='initialview01'>2cm0</scene>, resolution 1.9Å | |||
|SITE= <scene name='pdbsite=AC1:Bme+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CM0 is a [ | 2CM0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CM0 OCA]. | ||
==Reference== | ==Reference== | ||
The PUB domain functions as a p97 binding module in human peptide N-glycanase., Allen MD, Buchberger A, Bycroft M, J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. PMID:[http:// | The PUB domain functions as a p97 binding module in human peptide N-glycanase., Allen MD, Buchberger A, Bycroft M, J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16807242 16807242] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''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 16:17:04 2008'' | ||
Revision as of 14:17, 20 March 2008
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| 2cm0, resolution 1.9Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | BME and PEG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.
Overview
The AAA ATPase p97 is a ubiquitin-selective molecular machine involved in multiple cellular processes, including protein degradation through the ubiquitin-proteasome system and homotypic membrane fusion. Specific p97 functions are mediated by a variety of cofactors, among them peptide N-glycanase, an enzyme that removes glycans from misfolded glycoproteins. Here we report the three-dimensional structure of the aminoterminal PUB domain of human peptide N-glycanase. We demonstrate that the PUB domain is a novel p97 binding module interacting with the D1 and/or D2 ATPase domains of p97 and identify an evolutionary conserved surface patch required for p97 binding. Furthermore, we show that the PUB and UBX domains do not bind to p97 in a mutually exclusive manner. Our results suggest that PUB domain-containing proteins constitute a widespread family of diverse p97 cofactors.
About this Structure
2CM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The PUB domain functions as a p97 binding module in human peptide N-glycanase., Allen MD, Buchberger A, Bycroft M, J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. PMID:16807242
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