7AP8
Atomic structure of the poxvirus initially transcribing complex in conformation 2
Summary for 7AP8
Entry DOI | 10.2210/pdb7ap8/pdb |
EMDB information | 11850 |
Descriptor | DNA-directed RNA polymerase 147 kDa polypeptide, RNA (5'-R(P*AP*UP*AP*AP*A)-3'), DNA-directed RNA polymerase 30 kDa polypeptide, ... (14 entities in total) |
Functional Keywords | vaccinia, virus, rna polymerase, dna-dependent, initiation complex, pic, poxvirus, poxviridae, transcription |
Biological source | Vaccinia virus GLV-1h68 More |
Total number of polymer chains | 12 |
Total formula weight | 543887.75 |
Authors | Grimm, C.,Bartuli, J.,Fischer, U. (deposition date: 2020-10-16, release date: 2021-10-06, Last modification date: 2024-11-20) |
Primary citation | Grimm, C.,Bartuli, J.,Boettcher, B.,Szalay, A.A.,Fischer, U. Structural basis of the complete poxvirus transcription initiation process. Nat.Struct.Mol.Biol., 28:779-788, 2021 Cited by PubMed Abstract: Poxviruses express their genes in the cytoplasm of infected cells using a virus-encoded multi-subunit polymerase (vRNAP) and unique transcription factors. We present cryo-EM structures that uncover the complete transcription initiation phase of the poxvirus vaccinia. In the pre-initiation complex, the heterodimeric early transcription factor VETFs/l adopts an arc-like shape spanning the polymerase cleft and anchoring upstream and downstream promoter elements. VETFI emerges as a TBP-like protein that inserts asymmetrically into the DNA major groove, triggers DNA melting, ensures promoter recognition and enforces transcription directionality. The helicase VETFs fosters promoter melting and the phospho-peptide domain (PPD) of vRNAP subunit Rpo30 enables transcription initiation. An unprecedented upstream promoter scrunching mechanism assisted by the helicase NPH-I probably fosters promoter escape and transition into elongation. Our structures shed light on unique mechanisms of poxviral gene expression and aid the understanding of thus far unexplained universal principles in transcription. PubMed: 34556871DOI: 10.1038/s41594-021-00655-w PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.15 Å) |
Structure validation
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