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4BOC

Structure of mitochondrial RNA polymerase elongation complex

Summary for 4BOC
Entry DOI10.2210/pdb4boc/pdb
DescriptorDNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL, 5'-D(*CP*AP*TP*GP*GP*GP*GP*TP*AP*AP*TP*TP*AP*TP *TP*TP*CP*GP*AP*CP*GP*CP*CP*AP*GP*AP*CP*G)-3', 5'-R(*AP*GP*UP*CP*UP*GP*CP*GP*GP*CP*GP*CP*GP*CP)-3', ... (5 entities in total)
Functional Keywordstranscription, rna polymerase, mitochondria, transferase, dna-rna hybrid
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationMitochondrion: O00411
Total number of polymer chains4
Total formula weight145059.29
Authors
Schwinghammer, K.,Cheung, A.,Morozov, Y.,Agaronyan, K.,Temiakov, D.,Cramer, P. (deposition date: 2013-05-18, release date: 2013-09-25, Last modification date: 2023-12-20)
Primary citationSchwinghammer, K.,Cheung, A.C.M.,Morozov, Y.I.,Agaronyan, K.,Temiakov, D.,Cramer, P.
Structure of Human Mitochondrial RNA Polymerase Elongation Complex
Nat.Struct.Mol.Biol., 20:1298-, 2013
Cited by
PubMed Abstract: Here we report the crystal structure of the human mitochondrial RNA polymerase (mtRNAP) transcription elongation complex, determined at 2.65-Å resolution. The structure reveals a 9-bp hybrid formed between the DNA template and the RNA transcript and one turn of DNA both upstream and downstream of the hybrid. Comparisons with the distantly related RNA polymerase (RNAP) from bacteriophage T7 indicates conserved mechanisms for substrate binding and nucleotide incorporation but also strong mechanistic differences. Whereas T7 RNAP refolds during the transition from initiation to elongation, mtRNAP adopts an intermediary conformation that is capable of elongation without refolding. The intercalating hairpin that melts DNA during T7 RNAP initiation separates RNA from DNA during mtRNAP elongation. Newly synthesized RNA exits toward the pentatricopeptide repeat (PPR) domain, a unique feature of mtRNAP with conserved RNA-recognition motifs.
PubMed: 24096365
DOI: 10.1038/NSMB.2683
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

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