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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
  • 26
    Citations
  • 0
    Usage
  • 55
    Captures
  • 2
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    26
  • Captures
    55
  • Mentions
    2
    • News Mentions
      1
      • News
        1
    • References
      1
      • Wikipedia
        1

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

Liu, Gaohua; Forouhar, Farhad; Eletsky, Alexander; Atreya, Hanudatta S; Aramini, James M; Xiao, Rong; Huang, Yuanpeng J; Abashidze, Mariam; Seetharaman, Jayaraman; Liu, Jinfeng; Rost, Burkhard; Acton, Thomas; Montelione, Gaetano T; Hunt, John F; Szyperski, Thomas

Springer Science and Business Media LLC

Biochemistry, Genetics and Molecular Biology

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