6X50
Mfd-bound E.coli RNA polymerase elongation complex - V state
Summary for 6X50
| Entry DOI | 10.2210/pdb6x50/pdb |
| Related | 6X26 6X2F 6X2N 6X43 6X4W 6X4Y |
| EMDB information | 21996 22006 22012 22039 22043 22044 22045 |
| Descriptor | Transcription-repair-coupling factor, MAGNESIUM ION, ZINC ION, ... (11 entities in total) |
| Functional Keywords | transcription-coupled dna repair, dna translocase, elongation complex, rna polymerase, transcription, transcription-rna-dna complex, transcription/rna/dna |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 9 |
| Total formula weight | 566282.69 |
| Authors | Llewelyn, E.,Chen, J.,Kang, J.Y.,Darst, S.A. (deposition date: 2020-05-24, release date: 2021-02-03, Last modification date: 2024-03-06) |
| Primary citation | Kang, J.Y.,Llewellyn, E.,Chen, J.,Olinares, P.D.B.,Brewer, J.,Chait, B.T.,Campbell, E.A.,Darst, S.A. Structural basis for transcription complex disruption by the Mfd translocase. Elife, 10:-, 2021 Cited by PubMed Abstract: Transcription-coupled repair (TCR) is a sub-pathway of nucleotide excision repair (NER) that preferentially removes lesions from the template-strand (t-strand) that stall RNA polymerase (RNAP) elongation complexes (ECs). Mfd mediates TCR in bacteria by removing the stalled RNAP concealing the lesion and recruiting Uvr(A)BC. We used cryo-electron microscopy to visualize Mfd engaging with a stalled EC and attempting to dislodge the RNAP. We visualized seven distinct Mfd-EC complexes in both ATP and ADP-bound states. The structures explain how Mfd is remodeled from its repressed conformation, how the UvrA-interacting surface of Mfd is hidden during most of the remodeling process to prevent premature engagement with the NER pathway, how Mfd alters the RNAP conformation to facilitate disassembly, and how Mfd forms a processive translocation complex after dislodging the RNAP. Our results reveal an elaborate mechanism for how Mfd kinetically discriminates paused from stalled ECs and disassembles stalled ECs to initiate TCR. PubMed: 33480355DOI: 10.7554/eLife.62117 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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