8RAS
Plastid-encoded RNA polymerase transcription elongation complex
This is a non-PDB format compatible entry.
Summary for 8RAS
| Entry DOI | 10.2210/pdb8ras/pdb |
| EMDB information | 19023 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, PAP6, PAP7, ... (26 entities in total) |
| Functional Keywords | transcription, chloroplast, rna polymerase, photosynthesis, gene regulation |
| Biological source | Sinapis alba (white mustard) More |
| Total number of polymer chains | 23 |
| Total formula weight | 1277075.31 |
| Authors | Webster, M.W.,Pramanick, I.,Vergara-Cruces, A. (deposition date: 2023-12-01, release date: 2024-03-06, Last modification date: 2025-12-10) |
| Primary citation | Vergara-Cruces, A.,Pramanick, I.,Pearce, D.,Vogirala, V.K.,Byrne, M.J.,Low, J.K.K.,Webster, M.W. Structure of the plant plastid-encoded RNA polymerase. Cell, 187:1145-1159.e21, 2024 Cited by PubMed Abstract: Chloroplast genes encoding photosynthesis-associated proteins are predominantly transcribed by the plastid-encoded RNA polymerase (PEP). PEP is a multi-subunit complex composed of plastid-encoded subunits similar to bacterial RNA polymerases (RNAPs) stably bound to a set of nuclear-encoded PEP-associated proteins (PAPs). PAPs are essential to PEP activity and chloroplast biogenesis, but their roles are poorly defined. Here, we present cryoelectron microscopy (cryo-EM) structures of native 21-subunit PEP and a PEP transcription elongation complex from white mustard (Sinapis alba). We identify that PAPs encase the core polymerase, forming extensive interactions that likely promote complex assembly and stability. During elongation, PAPs interact with DNA downstream of the transcription bubble and with the nascent mRNA. The models reveal details of the superoxide dismutase, lysine methyltransferase, thioredoxin, and amino acid ligase enzymes that are subunits of PEP. Collectively, these data provide a foundation for the mechanistic understanding of chloroplast transcription and its role in plant growth and adaptation. PubMed: 38428394DOI: 10.1016/j.cell.2024.01.036 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.62 Å) |
Structure validation
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