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6ERO

Structure of human TFB2M

Summary for 6ERO
Entry DOI10.2210/pdb6ero/pdb
DescriptorDimethyladenosine transferase 2, mitochondrial,Dimethyladenosine transferase 2, mitochondrial, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsmitochondria, transcription, initiation, polymerase
Biological sourceHomo sapiens (Human)
More
Cellular locationMitochondrion: Q9H5Q4
Total number of polymer chains2
Total formula weight71690.33
Authors
Hillen, H.S.,Morozov, Y.I.,Sarfallah, A.,Temiakov, D.,Cramer, P. (deposition date: 2017-10-18, release date: 2017-11-15, Last modification date: 2024-05-01)
Primary citationHillen, H.S.,Morozov, Y.I.,Sarfallah, A.,Temiakov, D.,Cramer, P.
Structural Basis of Mitochondrial Transcription Initiation.
Cell, 171:1072-1081.e10, 2017
Cited by
PubMed Abstract: Transcription in human mitochondria is driven by a single-subunit, factor-dependent RNA polymerase (mtRNAP). Despite its critical role in both expression and replication of the mitochondrial genome, transcription initiation by mtRNAP remains poorly understood. Here, we report crystal structures of human mitochondrial transcription initiation complexes assembled on both light and heavy strand promoters. The structures reveal how transcription factors TFAM and TFB2M assist mtRNAP to achieve promoter-dependent initiation. TFAM tethers the N-terminal region of mtRNAP to recruit the polymerase to the promoter whereas TFB2M induces structural changes in mtRNAP to enable promoter opening and trapping of the DNA non-template strand. Structural comparisons demonstrate that the initiation mechanism in mitochondria is distinct from that in the well-studied nuclear, bacterial, or bacteriophage transcription systems but that similarities are found on the topological and conceptual level. These results provide a framework for studying the regulation of gene expression and DNA replication in mitochondria.
PubMed: 29149603
DOI: 10.1016/j.cell.2017.10.036
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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数据于2024-10-30公开中

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