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TitleOligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 6350, Year 2024
Publish dateJul 28, 2024
AuthorsXin Lan / Wei Huang / Su Bin Kim / Dechen Fu / Thilini Abeywansha / Jiemin Lou / Udayakumaran Balamurugan / Yong Tae Kwon / Chang Hoon Ji / Derek J Taylor / Yi Zhang /
PubMed AbstractThe arginyl-transferase ATE1 is a tRNA-dependent enzyme that covalently attaches an arginine molecule to a protein substrate. Conserved from yeast to humans, ATE1 deficiency in mice correlates with ...The arginyl-transferase ATE1 is a tRNA-dependent enzyme that covalently attaches an arginine molecule to a protein substrate. Conserved from yeast to humans, ATE1 deficiency in mice correlates with defects in cardiovascular development and angiogenesis and results in embryonic lethality, while conditional knockouts exhibit reproductive, developmental, and neurological deficiencies. Despite the recent revelation of the tRNA binding mechanism and the catalytic cycle of yeast ATE1, the structure-function relationship of ATE1 in higher organisms is not well understood. In this study, we present the three-dimensional structure of human ATE1 in an apo-state and in complex with its tRNA cofactor and a peptide substrate. In contrast to its yeast counterpart, human ATE1 forms a symmetric homodimer, which dissociates upon binding of a substrate. Furthermore, human ATE1 includes a unique and extended loop that wraps around tRNA, creating extensive contacts with the T-arm of the tRNA cofactor. Substituting key residues identified in the substrate binding site of ATE1 abolishes enzymatic activity and results in the accumulation of ATE1 substrates in cells.
External linksNat Commun / PubMed:39068213 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 5.7 Å
Structure data

41770

8tzv

EMDB-41770, PDB-8tzv:
Apo form of human ATE1
Method: EM (single particle) / Resolution: 2.8 Å

42071

8uau

EMDB-42071, PDB-8uau:
human ATE1 in complex with Arg-tRNA and a peptide substrate
Method: EM (single particle) / Resolution: 5.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / arginylation / ATE1 / apo / TRANSFERASE/RNA / complex / TRANSFERASE-RNA complex

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