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8CLK

TFIIIC TauA complex

This is a non-PDB format compatible entry.
Summary for 8CLK
Entry DOI10.2210/pdb8clk/pdb
EMDB information16715
DescriptorGeneral transcription factor 3C polypeptide 1, General transcription factor 3C polypeptide 3, General transcription factor 3C polypeptide 5, ... (4 entities in total)
Functional Keywordstfiiic, trna gene, b-box promoter, dna recognition, transcription
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight431127.11
Authors
Seifert-Davila, W.,Girbig, M.,Hauptmann, L.,Hoffmann, T.,Eustermann, S.,Mueller, C.W. (deposition date: 2023-02-16, release date: 2023-06-21, Last modification date: 2024-07-24)
Primary citationSeifert-Davila, W.,Girbig, M.,Hauptmann, L.,Hoffmann, T.,Eustermann, S.,Muller, C.W.
Structural insights into human TFIIIC promoter recognition.
Sci Adv, 9:eadh2019-eadh2019, 2023
Cited by
PubMed Abstract: Transcription factor (TF) IIIC recruits RNA polymerase (Pol) III to most of its target genes. Recognition of intragenic A- and B-box motifs in transfer RNA (tRNA) genes by TFIIIC modules τA and τB is the first critical step for tRNA synthesis but is mechanistically poorly understood. Here, we report cryo-electron microscopy structures of the six-subunit human TFIIIC complex unbound and bound to a tRNA gene. The τB module recognizes the B-box via DNA shape and sequence readout through the assembly of multiple winged-helix domains. TFIIIC220 forms an integral part of both τA and τB connecting the two subcomplexes via a ~550-amino acid residue flexible linker. Our data provide a structural mechanism by which high-affinity B-box recognition anchors TFIIIC to promoter DNA and permits scanning for low-affinity A-boxes and TFIIIB for Pol III activation.
PubMed: 37418517
DOI: 10.1126/sciadv.adh2019
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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