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TitleCryo-electron microscopy structure of a human PRMT5:MEP50 complex.
Journal, issue, pagesPLoS One, Vol. 13, Issue 3, Page e0193205, Year 2018
Publish dateMar 8, 2018
AuthorsDavid E Timm / Valorie Bowman / Russell Madsen / Charles Rauch /
PubMed AbstractProtein arginine methyl transferase 5 (PRMT5) is a signaling protein and histone modifying enzyme that is important in many cellular processes, including regulation of eukaryotic gene transcription. ...Protein arginine methyl transferase 5 (PRMT5) is a signaling protein and histone modifying enzyme that is important in many cellular processes, including regulation of eukaryotic gene transcription. Reported here is a 3.7 Å structure of PRMT5, solved in complex with regulatory binding subunit MEP50 (methylosome associated protein 50, WDR77, p44), by single particle (SP) cryo-Electron Microscopy (cryo-EM) using micrographs of particles that are visibly crowded and aggregated. Despite suboptimal micrograph appearance, this cryo-EM structure is in good agreement with previously reported crystal structures of the complex, which revealed a 450 kDa hetero-octameric assembly having internal D2 symmetry. The catalytic PRMT5 subunits form a core tetramer and the MEP50 subunits are arranged peripherally in complex with the PRMT5 N-terminal domain. The cryo-EM reconstruction shows good side chain definition and shows a well-resolved peak for a bound dehydrosinefungin inhibitor molecule. These results demonstrate the applicability of cryo-EM in determining structures of human protein complexes of biomedical significance and suggests cryo-EM could be further utilized to understand PRMT5 interactions with other biologically important binding proteins and ligands.
External linksPLoS One / PubMed:29518110 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

EMDB-7137:
PRMT5:MEP50 complex
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • Homo sapiens (human)

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