Structural basis for UFM1 transfer from UBA5 to UFC1
Ufmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process.
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-09-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-25994-6 |
| _version_ | 1823972899415916544 |
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| author | Manoj Kumar Prasanth Padala Jamal Fahoum Fouad Hassouna Tomer Tsaban Guy Zoltsman Sayanika Banerjee Einav Cohen-Kfir Moshe Dessau Rina Rosenzweig Michail N. Isupov Ora Schueler-Furman Reuven Wiener |
| author_facet | Manoj Kumar Prasanth Padala Jamal Fahoum Fouad Hassouna Tomer Tsaban Guy Zoltsman Sayanika Banerjee Einav Cohen-Kfir Moshe Dessau Rina Rosenzweig Michail N. Isupov Ora Schueler-Furman Reuven Wiener |
| author_sort | Manoj Kumar |
| collection | DOAJ |
| description | Ufmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process. |
| first_indexed | 2024-12-18T03:48:15Z |
| format | Article |
| id | doaj.art-92a7bec4aca04541b5ce9c87607504cd |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-18T03:48:15Z |
| publishDate | 2021-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-92a7bec4aca04541b5ce9c87607504cd2022-12-21T21:21:58ZengNature PortfolioNature Communications2041-17232021-09-0112111310.1038/s41467-021-25994-6Structural basis for UFM1 transfer from UBA5 to UFC1Manoj Kumar0Prasanth Padala1Jamal Fahoum2Fouad Hassouna3Tomer Tsaban4Guy Zoltsman5Sayanika Banerjee6Einav Cohen-Kfir7Moshe Dessau8Rina Rosenzweig9Michail N. Isupov10Ora Schueler-Furman11Reuven Wiener12Department of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolDepartment of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolDepartment of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolDepartment of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolDepartment of Microbiology and Molecular Genetics, Institute for Medical Research Israel-Canada, Faculty of Medicine, The Hebrew University of JerusalemDepartment of Chemical and Structural Biology, Weizmann Institute of SciencesDepartment of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolDepartment of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolAzrieli Faculty of Medicine, Bar-Ilan UniversityDepartment of Chemical and Structural Biology, Weizmann Institute of SciencesThe Henry Wellcome Building for Biocatalysis, Biosciences, University of ExeterDepartment of Microbiology and Molecular Genetics, Institute for Medical Research Israel-Canada, Faculty of Medicine, The Hebrew University of JerusalemDepartment of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical SchoolUfmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process.https://doi.org/10.1038/s41467-021-25994-6 |
| spellingShingle | Manoj Kumar Prasanth Padala Jamal Fahoum Fouad Hassouna Tomer Tsaban Guy Zoltsman Sayanika Banerjee Einav Cohen-Kfir Moshe Dessau Rina Rosenzweig Michail N. Isupov Ora Schueler-Furman Reuven Wiener Structural basis for UFM1 transfer from UBA5 to UFC1 Nature Communications |
| title | Structural basis for UFM1 transfer from UBA5 to UFC1 |
| title_full | Structural basis for UFM1 transfer from UBA5 to UFC1 |
| title_fullStr | Structural basis for UFM1 transfer from UBA5 to UFC1 |
| title_full_unstemmed | Structural basis for UFM1 transfer from UBA5 to UFC1 |
| title_short | Structural basis for UFM1 transfer from UBA5 to UFC1 |
| title_sort | structural basis for ufm1 transfer from uba5 to ufc1 |
| url | https://doi.org/10.1038/s41467-021-25994-6 |
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