Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural determinants for FAT10 activation and transfer from UBA6 to E2 enzymes.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Aug 13, 2026
Authors	Cara J Ellison / Carlos Riechmann / Evmorfia V Dalietou / Michael D R Simmons / Emma C Dodd / Paul R Elliott /
PubMed Abstract	Attachment of the ubiquitin-like protein (UBL) FAT10 onto substrates targets them for proteasomal degradation. Like ubiquitin, FAT10 is activated by the E1 enzyme UBA6 then transferred to E2 enzymes, ...Attachment of the ubiquitin-like protein (UBL) FAT10 onto substrates targets them for proteasomal degradation. Like ubiquitin, FAT10 is activated by the E1 enzyme UBA6 then transferred to E2 enzymes, but mechanisms controlling ubiquitin versus FAT10 activation by UBA6 and FAT10 transfer onto E2s remain unclear. Using cryo-EM, we visualise all stages of FAT10 E1-E2 handover: adenylation, thiolation and transthiolation. We find that FAT10 monopolises UBA6 by out-competing ubiquitin for thiolation and blocking the adenylation domain, preventing further UBL recruitment and promoting FAT10 signalling. We profiled UBA6-compatible E2 enzymes and found FAT10 transfer is restricted to a select subset associated with specific cellular pathways. UBE2Z (USE1) showed highest activity followed by UBE2D2, UBE2J2 and UBE2S. Capturing FAT10 or ubiquitin transfer from UBA6 to UBE2Z reveals UBE2Z is highly specialised for FAT10 transfer. It simultaneously engages both FAT10 domains (UBL1 and UBL2) and co-ordinates the metabolite inositol hexakisphosphate (InsP) bound within the UBA6 catalytic domain. This InsP co-ordination extends to other FAT10 compatible E2s. Together, our structural and biochemical analyses reveal regulatory mechanisms underpinning FAT10 activation and transfer. We define principles governing selective FAT10 transfer, highlighting favourable interactions with FAT10 C-terminal domain (UBL2) and stable UBA6 binding, ensuring controlled conjugation onto substrates.
External links	Nat Commun / PubMed:42733088 / PubMed Central
Methods	EM (single particle)
Resolution	2.77 - 3.53 Å
Structure data	56614 28mj EMDB-56614, PDB-28mj: Cryo-EM structure of UBA6 in complex with FAT10 in the pre-adenylation state. Method: EM (single particle) / Resolution: 2.77 Å 56615 28mk EMDB-56615, PDB-28mk: Cryo-EM structure of UBA6 in complex with FAT10 in the post-thiolation state. Method: EM (single particle) / Resolution: 3.53 Å 56644 28mo EMDB-56644, PDB-28mo: Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (singly loaded) Method: EM (single particle) / Resolution: 3.01 Å 56645 28mp EMDB-56645, PDB-28mp: Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (doubly loaded) Method: EM (single particle) / Resolution: 3.12 Å 56646 28mq EMDB-56646, PDB-28mq: Cryo-EM structure of UBA6-FAT10Dha-UBE2Z trapped ternary complex Method: EM (single particle) / Resolution: 3.04 Å
Chemicals	ChemComp-IHP: INOSITOL HEXAKISPHOSPHATE ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG*: Unknown entry
Source	homo sapiens (human)
Keywords	SIGNALING PROTEIN / Ubiquitin-activating enzyme / ubiquitin-like protein / adenylation / signalling cascade / ubiquitin