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Structure paper

TitleStructure of the TXNL1-bound proteasome.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 12, Page 2398-2402, Year 2025
Publish dateAug 6, 2025
AuthorsJingjing Gao / Christopher Nardone / Matthew C J Yip / Haruka Chino / Xin Gu / Zachary Mirman / Michael J Rale / Joao A Paulo / Stephen J Elledge / Sichen Shao /
PubMed AbstractProteasomes degrade diverse proteins in different cellular contexts through incompletely defined regulatory mechanisms. Here we report the cryo-EM structure of human thioredoxin-like protein 1 (TXNL1) ...Proteasomes degrade diverse proteins in different cellular contexts through incompletely defined regulatory mechanisms. Here we report the cryo-EM structure of human thioredoxin-like protein 1 (TXNL1) bound to the 19S regulatory particle of proteasomes via interactions with PSMD1 (Rpn2), PSMD4 (Rpn10) and PSMD14 (Rpn11). Proteasome binding is necessary for the ubiquitin-independent degradation of TXNL1 upon cellular exposure to metal- or metalloid-containing oxidative agents, thereby establishing a structural requirement for the stress-induced degradation of TXNL1.
External linksNat Struct Mol Biol / PubMed:40770113 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.3 Å
Structure data

EMDB-44949: TXNL1-bound proteasome (focused on TXNL1)
Method: EM (single particle) / Resolution: 3.0 Å

44952

9bw4

EMDB-44952, PDB-9bw4:
TXNL1-bound proteasome
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsNUCLEAR PROTEIN / proteasome

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