NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiquination pathway
Journal of Structural and Functional Genomics, ISSN: 1345-711X, Vol: 10, Issue: 2, Page: 127-136
2009
- 26Citations
- 55Captures
- 2Mentions
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- Citations26
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- 26
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- 55
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Most Recent News
The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons
Nature, Published online: 21 February 2024; doi:10.1038/s41586-024-07093-w Attachment of the ubiquitin-like modifier UFM1 to 60S ribosomes has a critical function in the release and recycling of stalled or terminated ribosomes from the endoplasmic reticulum membrane.
Article Description
For cell regulation, E2-like ubiquitin-fold modifier conjugating enzyme 1 (Ufc1) is involved in the transfer of ubiquitin-fold modifier 1 (Ufm1), a ubiquitin like protein which is activated by E1-like enzyme Uba5, to various target proteins. Thereby, Ufc1 participates in the very recently discovered Ufm1-Uba5-Ufc1 ubiquination pathway which is found in metazoan organisms. The structure of human Ufc1 was solved by using both NMR spectroscopy and X-ray crystallography. The complementary insights obtained with the two techniques provided a unique basis for understanding the function of Ufc1 at atomic resolution. The Ufc1 structure consists of the catalytic core domain conserved in all E2-like enzymes and an additional N-terminal helix. The active site Cys, which forms a thio-ester bond with Ufm1, is located in a flexible loop that is highly solvent accessible. Based on the Ufc1 and Ufm1 NMR structures, a model could be derived for the Ufc1-Ufm1 complex in which the C-terminal Gly of Ufm1 may well form the expected thio-ester with Cys, suggesting that Ufm1-Ufc1 functions as described for other E1-E2-E3 machineries. α-helix 1 of Ufc1 adopts different conformations in the crystal and in solution, suggesting that this helix plays a key role to mediate specificity. © 2008 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=62949100271&origin=inward; http://dx.doi.org/10.1007/s10969-008-9054-7; http://www.ncbi.nlm.nih.gov/pubmed/19101823; http://link.springer.com/10.1007/s10969-008-9054-7; https://dx.doi.org/10.1007/s10969-008-9054-7; https://link.springer.com/article/10.1007/s10969-008-9054-7; http://www.springerlink.com/index/10.1007/s10969-008-9054-7; http://www.springerlink.com/index/pdf/10.1007/s10969-008-9054-7
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