7nvj

Crystal structure of UFC1 Y110A & F121A

spinqualitylabelsall models 7nvj, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7nvj is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UFC1_HUMAN E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage. Publication Abstract from PubMed Ufmylation is a post-translational modification essential for regulating key cellular processes. A three-enzyme cascade involving E1, E2 and E3 is required for UFM1 attachment to target proteins. How UBA5 (E1) and UFC1 (E2) cooperatively activate and transfer UFM1 is still unclear. Here, we present the crystal structure of UFC1 bound to the C-terminus of UBA5, revealing how UBA5 interacts with UFC1 via a short linear sequence, not observed in other E1-E2 complexes. We find that UBA5 has a region outside the adenylation domain that is dispensable for UFC1 binding but critical for UFM1 transfer. This region moves next to UFC1's active site Cys and compensates for a missing loop in UFC1, which exists in other E2s and is needed for the transfer. Overall, our findings advance the understanding of UFM1's conjugation machinery and may serve as a basis for the development of ufmylation inhibitors. Structural basis for UFM1 transfer from UBA5 to UFC1.,Kumar M, Padala P, Fahoum J, Hassouna F, Tsaban T, Zoltsman G, Banerjee S, Cohen-Kfir E, Dessau M, Rosenzweig R, Isupov MN, Schueler-Furman O, Wiener R Nat Commun. 2021 Sep 29;12(1):5708. doi: 10.1038/s41467-021-25994-6. PMID:34588452 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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