Figure 5
From: Novel insights into the interaction of UBA5 with UFM1 via a UFM1-interacting sequence
Structural analysis of UFM1 crystal structure. (A) Crystal structure of UFM1 showing the beta grasp fold commonly observed in ubiquitin and other UBLs. The asymmetric unit contains two molecules of UFM1. (B) Contact between two UFM1 molecules in asymmetric unit mimics the UIS binding to UFM1. Superposition between UFM1-UIS structure and UFM1 alone; the UIS is in blue. The spatial position of UIS H336 and I343 overlap with UFM1 H70 and I55, respectively. (C) Gel filtration elution profiles of UFM1 WT or mutants. (D) Superposition of UFM1 dimer (orange) with UBA5-UFM1 complex. UBA5 (red) holds the UFM1 dimer in an orientation that generates clashes with the UFM1 molecule that does not interact with the UIS and the adenylation domain, thereby preventing charging of UFM1 dimer.
