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8XZV

Architecture of the spinach plastid-encoded RNA polymerase

Summary for 8XZV
Entry DOI10.2210/pdb8xzv/pdb
EMDB information38799
DescriptorDNA-directed RNA polymerase subunit alpha, pTAC6, superoxide dismutase, ... (18 entities in total)
Functional Keywordsplastid-encoded rna polymerase, chloroplast, spinach, transcription
Biological sourceSpinacia oleracea (spinach)
More
Total number of polymer chains19
Total formula weight1112543.21
Authors
Wang, G.-L.,Yu, L.-J.,Lu, C. (deposition date: 2024-01-21, release date: 2024-12-04)
Primary citationWang, T.,Wang, G.L.,Fang, Y.,Zhang, Y.,Peng, W.,Zhou, Y.,Zhang, A.,Yu, L.J.,Lu, C.
Architecture of the spinach plastid-encoded RNA polymerase.
Nat Commun, 15:9838-9838, 2024
Cited by
PubMed Abstract: The plastid-encoded RNA polymerase serves as the principal transcription machinery within chloroplasts, transcribing over 80% of all primary plastid transcripts. This polymerase consists of a prokaryotic-like core enzyme known as the plastid-encoded RNA polymerase core, and is supplemented by newly evolved associated proteins known as PAPs. However, the architecture of the plastid-encoded RNA polymerase and the possible functions of PAPs remain unknown. Here, we present the cryo-electron microscopy structure of a 19-subunit plastid-encoded RNA polymerase complex derived from spinach (Spinacia oleracea). The structure shows that the plastid-encoded RNA polymerase core resembles bacterial RNA polymerase. Twelve PAPs and two additional proteins (FLN2 and pTAC18) bind at the periphery of the plastid-encoded RNA polymerase core, forming extensive interactions that may facilitate complex assembly and stability. PAPs may also protect the complex against oxidative damage and has potential functions in transcriptional regulation. This research offers a structural basis for future investigations into the functions and regulatory mechanisms governing the transcription of plastid genes.
PubMed: 39537621
DOI: 10.1038/s41467-024-54266-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.16 Å)
Structure validation

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