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Structure paper

TitleStructural basis of co-translational N-myristoylation in humans.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Page 1191, Year 2026
Publish dateJan 23, 2026
AuthorsTimo Denk / Paul Monassa / Joanna Musial / Otto Berninghausen / Birgitta Beatrix / Carmela Giglione / Thierry Meinnel / Roland Beckmann /
PubMed AbstractModifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co- ...Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co-translationally by N-myristoyltransferases (NMTs) which have been identified as promising drug targets. However, its molecular basis in the context of the translating ribosome is not known. Here, we reveal the structural basis for co-translational N-myristoylation by NMT1 on the human ribosome by cryo-electron microscopy (cryo-EM). We show that NMT1 binds near the peptide tunnel exit and interacts with the nascent polypeptide-associated complex (NAC). Unlike other multi-enzyme complexes that act simultaneously, we find that methionine excision by methionine aminopeptidases and N-myristoylation occur sequentially via consecutive binding to the ribosome. Furthermore, our data suggest that NMT1 remains associated with elongating nascent chains, indicating a co-translational chaperone-like function in partnership with NAC. These insights provide a molecular foundation for the understanding of the co-translational N-myristoylation mechanism in humans.
External linksNat Commun / PubMed:41577716 / PubMed Central
MethodsEM (single particle)
Resolution2.19 - 2.95 Å
Structure data

52581

9i2d

EMDB-52581, PDB-9i2d:
NMT1-NAC bound human RNC with 10 amino acid ARF1-linker
Method: EM (single particle) / Resolution: 2.19 Å

52582

9i2e

EMDB-52582, PDB-9i2e:
NMT1-NAC bound human ribosome (combined translational states)
Method: EM (single particle) / Resolution: 2.95 Å

53230

9qlo

EMDB-53230, PDB-9qlo:
NMT1-NAC bound human RNC with full length ARF1 - State 1
Method: EM (single particle) / Resolution: 2.47 Å

53231

9qlp

EMDB-53231, PDB-9qlp:
NMT1-NAC bound human RNC with full length ARF1 - State 2
Method: EM (single particle) / Resolution: 2.75 Å

53232

9qlq

EMDB-53232, PDB-9qlq:
NMT1-NAC bound human RNC with full length ARF1 - alternative State
Method: EM (single particle) / Resolution: 2.57 Å

54528

9s3b

EMDB-54528, PDB-9s3b:
NMT1-NAC bound human RNC with 58 amino acid ARF1-linker - State 1
Method: EM (single particle) / Resolution: 2.38 Å

54529

9s3c

EMDB-54529, PDB-9s3c:
NMT1-NAC bound human RNC with 58 amino acid ARF1-linker - State 2
Method: EM (single particle) / Resolution: 2.42 Å

54530

9s3d

EMDB-54530, PDB-9s3d:
NAC bound human RNC with 58 amino acid ARF1-linker
Method: EM (single particle) / Resolution: 2.32 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-G3D:
GUANOSINE-3'-MONOPHOSPHATE-5'-DIPHOSPHATE

Source
  • homo sapiens (human)
KeywordsRIBOSOME / myristoylation / NMT1 / co-translational / NAC / RNC / N-terminal myristoylation / ARF1

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