4BJI

Sfc1-DBD

Summary for 4BJI

• Entry DOI: 10.2210/pdb4bji/pdb
• Related: 4BJJ
• Descriptor: TRANSCRIPTION FACTOR TAU SUBUNIT SFC1 (2 entities in total)
• Functional Keywords: dna binding protein
• Biological source: SCHIZOSACCHAROMYCES POMBE (FISSION YEAST)
• Cellular location: Nucleus (By similarity): O14229
• Total number of polymer chains: 1
• Total formula weight: 25178.12

Authors

Taylor, N.M.I.,Baudin, F.,von Scheven, G.,Muller, C.W. (deposition date: 2013-04-18, release date: 2013-07-31, Last modification date: 2024-11-13)

Primary citation

Taylor, N.M.I.,Baudin, F.,Von Scheven, G.,Muller, C.W.
RNA Polymerase III-Specific General Transcription Factor Iiic Contains a Heterodimer Resembling Tfiif RAP30/RAP74.
Nucleic Acids Res., 41:9183-, 2013

PubMed Abstract: Transcription of tRNA-encoding genes by RNA polymerase (Pol) III requires the six-subunit general transcription factor IIIC that uses subcomplexes τA and τB to recognize two gene-internal promoter elements named A- and B-box. The Schizosaccharomyces pombe τA subcomplex comprises subunits Sfc1, Sfc4 and Sfc7. The crystal structure of the Sfc1/Sfc7 heterodimer reveals similar domains and overall domain architecture to the Pol II-specific general transcription factor TFIIF Rap30/Rap74. The N-terminal Sfc1/Sfc7 dimerization module consists of a triple β-barrel similar to the N-terminal TFIIF Rap30/Rap74 dimerization module, whereas the C-terminal Sfc1 DNA-binding domain contains a winged-helix domain most similar to the TFIIF Rap30 C-terminal winged-helix domain. Sfc1 DNA-binding domain recognizes single and double-stranded DNA by an unknown mechanism. Several features observed for A-box recognition by τA resemble the recognition of promoters by bacterial RNA polymerase, where σ factor unfolds double-stranded DNA and stabilizes the non-coding DNA strand in an open conformation. Such a function has also been proposed for TFIIF, suggesting that the observed structural similarity between Sfc1/Sfc7 and TFIIF Rap30/Rap74 might also reflect similar functions.

PubMed: 23921640
DOI: 10.1093/NAR/GKT664

Experimental method

X-RAY DIFFRACTION (1.45 Å)