Ubiquitin conjugating enzyme
From Proteopedia
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| - | <StructureSection load='3ptf' size='350' side='right' caption='Structure of human ubiquitin conjugating enzyme E2 (grey | + | <StructureSection load='3ptf' size='350' side='right' caption='Structure of human ubiquitin conjugating enzyme E2 (grey) complex with ubiquitin (pink) (PDB entry [[3ptf]])' scene=''> |
| - | + | == Function == | |
'''Ubiquitin conjugating enzyme''' (Ubc) or '''E2 enzyme''' catalyzes the second step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (E2) (Ubc) cysteine<ref>PMID:19549727</ref>. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. Ubc13 makes a catalytically active heterodimer with MMS2.<br /> | '''Ubiquitin conjugating enzyme''' (Ubc) or '''E2 enzyme''' catalyzes the second step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (E2) (Ubc) cysteine<ref>PMID:19549727</ref>. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. Ubc13 makes a catalytically active heterodimer with MMS2.<br /> | ||
For more details on Ubc13 see [[UBC13 MMS2]].<br /> | For more details on Ubc13 see [[UBC13 MMS2]].<br /> | ||
For more details on Ubc9 see [[Ubc9]].<br /> | For more details on Ubc9 see [[Ubc9]].<br /> | ||
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| + | == Structural highlights == | ||
| + | There are 2 distinct interactions between Ubc and ubiquitin. The first involves hydrophobic interactions between the area in Ubc around Ser22 and the ubiquitin I44. The second involves the contact between residues near the Ubc active site Cys85 and the ubiquitin TEK box<ref>PMID:21396940</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:25, 30 November 2016
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3D Structures of ubiquitin conjugating enzyme
Updated on 30-November-2016
References
- ↑ Markson G, Kiel C, Hyde R, Brown S, Charalabous P, Bremm A, Semple J, Woodsmith J, Duley S, Salehi-Ashtiani K, Vidal M, Komander D, Serrano L, Lehner P, Sanderson CM. Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network. Genome Res. 2009 Oct;19(10):1905-11. Epub 2009 Jun 23. PMID:19549727 doi:http://dx.doi.org/gr.093963.109
- ↑ Bosanac I, Phu L, Pan B, Zilberleyb I, Maurer B, Dixit VM, Hymowitz SG, Kirkpatrick DS. Modulation of K11-Linkage Formation by Variable Loop Residues within UbcH5A. J Mol Biol. 2011 May 6;408(3):420-31. Epub 2011 Mar 10. PMID:21396940 doi:10.1016/j.jmb.2011.03.011
