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TitleCryo-EM structures reveal the molecular mechanism of SUMO E1-E2 thioester transfer.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 12, Page 2441-2453, Year 2025
Publish dateSep 25, 2025
AuthorsAnindita Nayak / Digant Nayak / Lijia Jia / Eliza A Ruben / Suryavathi Viswanadhapalli / Priscila Dos Santos Bury / Khaled Mohamed Nassar / Corey H Yu / Anna A Tumanova / Caleb M Stratton / Pirouz Ebadi / Dmitri N Ivanov / Patrick Sung / Ratna K Vadlamudi / Elizabeth V Wasmuth / Shaun K Olsen /
PubMed AbstractPost-translational modification of proteins by SUMO (small ubiquitin-like modifier) regulates fundamental cellular processes and occurs through the sequential interactions and activities of three ...Post-translational modification of proteins by SUMO (small ubiquitin-like modifier) regulates fundamental cellular processes and occurs through the sequential interactions and activities of three enzymes: E1, E2 and E3. SUMO E1 activates SUMO in a two-step process involving adenylation and thioester bond formation, followed by transfer of SUMO to its dedicated E2 enzyme, UBC9. This process is termed E1-E2 thioester transfer (or transthioesterification). Despite its fundamental importance, the molecular basis for SUMO E1-UBC9 thioester transfer and the molecular rules governing SUMO E1-UBC9 specificity are poorly understood. Here we present cryo-EM reconstructions of human SUMO E1 in complex with UBC9, SUMO1 adenylate and SUMO1 thioester intermediate. Our structures reveal drastic conformational changes that accompany thioester transfer, providing insights into the molecular recognition of UBC9 by SUMO E1 and delineating the rules that govern SUMO E1-UBC9 specificity. Collectively, our structural, biochemical and cell-based studies elucidate the molecular mechanisms by which SUMOylation exerts its essential biological functions.
External linksNat Struct Mol Biol / PubMed:40999065 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.6 Å
Structure data

47110

9dqb

EMDB-47110, PDB-9dqb:
Cryo-EM structure of a double-loaded SUMO E1-E2-SUMO1 complex.
Method: EM (single particle) / Resolution: 3.6 Å

47127

9drj

EMDB-47127, PDB-9drj:
Cryo-EM structure of a SUMO E1-E2-SUMO1 complex.
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / Sumo1(a) / Sumo1(t) / sae1 / ubc9 / uba2 / Sumo1

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