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7ASV

Crystal structure of tWHD2 of Rpc5 subunit of human RNA Polymerase III

Summary for 7ASV
Entry DOI10.2210/pdb7asv/pdb
DescriptorDNA-directed RNA polymerase III subunit RPC5, ACETATE ION (3 entities in total)
Functional Keywordsrna pol iii, rna polymerase iii, transcription, rpc5
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight162268.12
Authors
Vannini, A.,Abascal-Palacios, G.,Ramsay, E.P. (deposition date: 2020-10-28, release date: 2020-12-30, Last modification date: 2024-10-09)
Primary citationRamsay, E.P.,Abascal-Palacios, G.,Daiss, J.L.,King, H.,Gouge, J.,Pilsl, M.,Beuron, F.,Morris, E.,Gunkel, P.,Engel, C.,Vannini, A.
Structure of human RNA polymerase III.
Nat Commun, 11:6409-6409, 2020
Cited by
PubMed Abstract: In eukaryotes, RNA Polymerase (Pol) III is specialized for the transcription of tRNAs and other short, untranslated RNAs. Pol III is a determinant of cellular growth and lifespan across eukaryotes. Upregulation of Pol III transcription is observed in cancer and causative Pol III mutations have been described in neurodevelopmental disorders and hypersensitivity to viral infection. Here, we report a cryo-EM reconstruction at 4.0 Å of human Pol III, allowing mapping and rationalization of reported genetic mutations. Mutations causing neurodevelopmental defects cluster in hotspots affecting Pol III stability and/or biogenesis, whereas mutations affecting viral sensing are located in proximity to DNA binding regions, suggesting an impairment of Pol III cytosolic viral DNA-sensing. Integrating x-ray crystallography and SAXS, we also describe the structure of the higher eukaryote specific RPC5 C-terminal extension. Surprisingly, experiments in living cells highlight a role for this module in the assembly and stability of human Pol III.
PubMed: 33335104
DOI: 10.1038/s41467-020-20262-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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数据于2025-07-23公开中

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