8QMA
Structure of the plastid-encoded RNA polymerase complex (PEP) from Sinapis alba
This is a non-PDB format compatible entry.
Summary for 8QMA
| Entry DOI | 10.2210/pdb8qma/pdb |
| EMDB information | 18496 |
| Descriptor | PAP4, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta'', ... (20 entities in total) |
| Functional Keywords | transcription, chloroplasts, gene expression, rna, polymerase |
| Biological source | Sinapis alba More |
| Total number of polymer chains | 19 |
| Total formula weight | 1117948.92 |
| Authors | do Prado, P.F.V.,Ahrens, F.M.,Pfannschmidt, T.,Hillen, H.S. (deposition date: 2023-09-21, release date: 2024-03-06, Last modification date: 2024-11-20) |
| Primary citation | do Prado, P.F.V.,Ahrens, F.M.,Liebers, M.,Ditz, N.,Braun, H.P.,Pfannschmidt, T.,Hillen, H.S. Structure of the multi-subunit chloroplast RNA polymerase. Mol.Cell, 84:910-, 2024 Cited by PubMed Abstract: Chloroplasts contain a dedicated genome that encodes subunits of the photosynthesis machinery. Transcription of photosynthesis genes is predominantly carried out by a plastid-encoded RNA polymerase (PEP), a nearly 1 MDa complex composed of core subunits with homology to eubacterial RNA polymerases (RNAPs) and at least 12 additional chloroplast-specific PEP-associated proteins (PAPs). However, the architecture of this complex and the functions of the PAPs remain unknown. Here, we report the cryo-EM structure of a 19-subunit PEP complex from Sinapis alba (white mustard). The structure reveals that the PEP core resembles prokaryotic and nuclear RNAPs but contains chloroplast-specific features that mediate interactions with the PAPs. The PAPs are unrelated to known transcription factors and arrange around the core in a unique fashion. Their structures suggest potential functions during transcription in the chemical environment of chloroplasts. These results reveal structural insights into chloroplast transcription and provide a framework for understanding photosynthesis gene expression. PubMed: 38428434DOI: 10.1016/j.molcel.2024.02.003 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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