7VBB
Structure of the post state human RNA Polymerase I Elongation Complex
This is a non-PDB format compatible entry.
Summary for 7VBB
Entry DOI | 10.2210/pdb7vbb/pdb |
EMDB information | 31877 |
Descriptor | DNA-directed RNA polymerase I subunit RPA1, DNA-directed RNA polymerases I, II, and III subunit RPABC4, DNA-directed RNA polymerase I subunit RPA34, ... (18 entities in total) |
Functional Keywords | rna polymerase i, transcription, post state, transcription-dna-rna complex, transcription/dna/rna |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 16 |
Total formula weight | 617396.32 |
Authors | |
Primary citation | Zhao, D.,Liu, W.,Chen, K.,Wu, Z.,Yang, H.,Xu, Y. Structure of the human RNA polymerase I elongation complex. Cell Discov, 7:97-97, 2021 Cited by PubMed Abstract: Eukaryotic RNA polymerase I (Pol I) transcribes ribosomal DNA and generates RNA for ribosome synthesis. Pol I accounts for the majority of cellular transcription activity and dysregulation of Pol I transcription leads to cancers and ribosomopathies. Despite extensive structural studies of yeast Pol I, structure of human Pol I remains unsolved. Here we determined the structures of the human Pol I in the pre-translocation, post-translocation, and backtracked states at near-atomic resolution. The single-subunit peripheral stalk lacks contacts with the DNA-binding clamp and is more flexible than the two-subunit stalk in yeast Pol I. Compared to yeast Pol I, human Pol I possesses a more closed clamp, which makes more contacts with DNA. The Pol I structure in the post-cleavage backtracked state shows that the C-terminal zinc ribbon of RPA12 inserts into an open funnel and facilitates "dinucleotide cleavage" on mismatched DNA-RNA hybrid. Critical disease-associated mutations are mapped on Pol I regions that are involved in catalysis and complex organization. In summary, the structures provide new sights into human Pol I complex organization and efficient proofreading. PubMed: 34671025DOI: 10.1038/s41421-021-00335-5 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.81 Å) |
Structure validation
Download full validation report
