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2cm0

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Revision as of 18:47, 24 January 2018

The PUB domain functions as a p97 binding module in human peptide N-glycanase.

Structural highlights

2cm0 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2ccq
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[NGLY1_HUMAN] Alacrimia-choreoathetosis-liver dysfunction syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

[NGLY1_HUMAN] Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Blom D, Hirsch C, Stern P, Tortorella D, Ploegh HL. A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J. 2004 Feb 11;23(3):650-8. Epub 2004 Jan 29. PMID:14749736 doi:http://dx.doi.org/10.1038/sj.emboj.7600090
↑ Katiyar S, Li G, Lennarz WJ. A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins. Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13774-9. Epub 2004 Sep 9. PMID:15358861 doi:http://dx.doi.org/10.1073/pnas.0405663101
↑ Allen MD, Buchberger A, Bycroft M. The PUB domain functions as a p97 binding module in human peptide N-glycanase. J Biol Chem. 2006 Sep 1;281(35):25502-8. Epub 2006 Jun 28. PMID:16807242 doi:10.1074/jbc.M601173200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cm0"

@@ Line 1: / Line 1: @@
-==THE PUB DOMAIN FUNCTIONS AS A P97 BINDING MODULE IN HUMAN PEPTIDE N-GLYCANASE.==
+==The PUB domain functions as a p97 binding module in human peptide N-glycanase.==
 <StructureSection load='2cm0' size='340' side='right' caption='[[2cm0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ccq|2ccq]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2cm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cm0 RCSB], [http://www.ebi.ac.uk/pdbsum/2cm0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2cm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cm0 RCSB], [http://www.ebi.ac.uk/pdbsum/2cm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cm0 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/2cm0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/2cm0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 2cm0" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Peptide N-glycanase|Peptide N-glycanase]]
 == References ==
 <references/>

2cm0

From Proteopedia

Revision as of 18:47, 24 January 2018

The PUB domain functions as a p97 binding module in human peptide N-glycanase.

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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