2cm0
From Proteopedia
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|PDB= 2cm0 |SIZE=350|CAPTION= <scene name='initialview01'>2cm0</scene>, resolution 1.9Å | |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> | |SITE= <scene name='pdbsite=AC1:Bme+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cm0 OCA], [http://www.ebi.ac.uk/pdbsum/2cm0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cm0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Buchberger, A.]] | [[Category: Buchberger, A.]] | ||
[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: PEG]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
[[Category: pug domain]] | [[Category: pug domain]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:23:21 2008'' |
Revision as of 23:23, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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