3m62
From Proteopedia
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{{STRUCTURE_3m62| PDB=3m62 | SCENE= }} | {{STRUCTURE_3m62| PDB=3m62 | SCENE= }} | ||
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===Crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) domain of Rad23=== | ===Crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) domain of Rad23=== | ||
| + | {{ABSTRACT_PUBMED_20427284}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/UFD2_YEAST UFD2_YEAST]] E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to CDC48 and elongates mono- and diubiquitinated ERAD substrates presented by the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrates to RAD23 and DSK2, which target them to the proteasome. Has E3 ubiquitin-protein ligase activity, accepting ubiquitin from its cognate E2 ubiquitin-conjugating enzyme UBC4. Enhances ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety. Promotes ubiquitin chain elongation at 'Lys-48' on the DOA10 substrate PEX29. Also involved in the proteolytic processing of the ER-bound transcription factor SPT23.<ref>PMID:10089879</ref> <ref>PMID:15240124</ref> <ref>PMID:15652483</ref> <ref>PMID:18191224</ref> <ref>PMID:20159987</ref> [[http://www.uniprot.org/uniprot/RAD23_YEAST RAD23_YEAST]] Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes. | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3m62]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M62 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020427284</ref><references group="xtra"/><references/> |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Haenzelmann, P.]] | [[Category: Haenzelmann, P.]] | ||
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[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Ubl conjugation pathway]] | [[Category: Ubl conjugation pathway]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 7 08:07:58 2010'' | ||
Revision as of 23:32, 10 April 2013
Contents |
Crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) domain of Rad23
Template:ABSTRACT PUBMED 20427284
Function
[UFD2_YEAST] E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to CDC48 and elongates mono- and diubiquitinated ERAD substrates presented by the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrates to RAD23 and DSK2, which target them to the proteasome. Has E3 ubiquitin-protein ligase activity, accepting ubiquitin from its cognate E2 ubiquitin-conjugating enzyme UBC4. Enhances ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety. Promotes ubiquitin chain elongation at 'Lys-48' on the DOA10 substrate PEX29. Also involved in the proteolytic processing of the ER-bound transcription factor SPT23.[1] [2] [3] [4] [5] [RAD23_YEAST] Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.
About this Structure
3m62 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
- Hanzelmann P, Stingele J, Hofmann K, Schindelin H, Raasi S. The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain. J Biol Chem. 2010 Jun 25;285(26):20390-8. Epub 2010 Apr 28. PMID:20427284 doi:10.1074/jbc.M110.112532
- ↑ Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell. 1999 Mar 5;96(5):635-44. PMID:10089879
- ↑ Saeki Y, Tayama Y, Toh-e A, Yokosawa H. Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage. Biochem Biophys Res Commun. 2004 Jul 30;320(3):840-5. PMID:15240124 doi:10.1016/j.bbrc.2004.05.216
- ↑ Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell. 2005 Jan 14;120(1):73-84. PMID:15652483 doi:10.1016/j.cell.2004.11.013
- ↑ Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell. 2008 Jan 11;132(1):101-12. doi: 10.1016/j.cell.2007.11.023. PMID:18191224 doi:10.1016/j.cell.2007.11.023
- ↑ Liu C, van Dyk D, Xu P, Choe V, Pan H, Peng J, Andrews B, Rao H. Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates. J Biol Chem. 2010 Apr 2;285(14):10265-72. Epub 2010 Feb 16. PMID:20159987 doi:M110.110551
