8WA1
The cryo-EM structure of the Nicotiana tabacum PEP-PAP-TEC2
This is a non-PDB format compatible entry.
Summary for 8WA1
| Entry DOI | 10.2210/pdb8wa1/pdb |
| EMDB information | 37388 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14-like isoform X2, PAP8(pTAC6), ... (24 entities in total) |
| Functional Keywords | transcription, pep, pap |
| Biological source | Nicotiana tabacum (common tobacco) More |
| Total number of polymer chains | 23 |
| Total formula weight | 1249620.04 |
| Authors | |
| Primary citation | Wu, X.X.,Mu, W.H.,Li, F.,Sun, S.Y.,Cui, C.J.,Kim, C.,Zhou, F.,Zhang, Y. Cryo-EM structures of the plant plastid-encoded RNA polymerase. Cell, 187:1127-1144.e21, 2024 Cited by PubMed Abstract: Chloroplasts are green plastids in the cytoplasm of eukaryotic algae and plants responsible for photosynthesis. The plastid-encoded RNA polymerase (PEP) plays an essential role during chloroplast biogenesis from proplastids and functions as the predominant RNA polymerase in mature chloroplasts. The PEP-centered transcription apparatus comprises a bacterial-origin PEP core and more than a dozen eukaryotic-origin PEP-associated proteins (PAPs) encoded in the nucleus. Here, we determined the cryo-EM structures of Nicotiana tabacum (tobacco) PEP-PAP apoenzyme and PEP-PAP transcription elongation complexes at near-atomic resolutions. Our data show the PEP core adopts a typical fold as bacterial RNAP. Fifteen PAPs bind at the periphery of the PEP core, facilitate assembling the PEP-PAP supercomplex, protect the complex from oxidation damage, and likely couple gene transcription with RNA processing. Our results report the high-resolution architecture of the chloroplast transcription apparatus and provide the structural basis for the mechanistic and functional study of transcription regulation in chloroplasts. PubMed: 38428393DOI: 10.1016/j.cell.2024.01.026 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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