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4XLQ

Crystal structure of T.aquaticus transcription initiation complex containing upstream fork (-11 base-paired) promoter

Summary for 4XLQ
Entry DOI10.2210/pdb4xlq/pdb
Related4XAX 4XLN 4XLP 4XLQ 4XLR
DescriptorDNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total)
Functional Keywordsprotein-dna complex, bacterial transcription initiation complex, transcription-dna complex, transcription/dna
Biological sourceThermus aquaticus
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Total number of polymer chains16
Total formula weight869245.49
Authors
Bae, B.,Darst, S.A. (deposition date: 2015-01-13, release date: 2015-09-23, Last modification date: 2024-11-20)
Primary citationBae, B.,Feklistov, A.,Lass-Napiorkowska, A.,Landick, R.,Darst, S.A.
Structure of a bacterial RNA polymerase holoenzyme open promoter complex.
Elife, 4:-, 2015
Cited by
PubMed Abstract: Initiation of transcription is a primary means for controlling gene expression. In bacteria, the RNA polymerase (RNAP) holoenzyme binds and unwinds promoter DNA, forming the transcription bubble of the open promoter complex (RPo). We have determined crystal structures, refined to 4.14 Å-resolution, of RPo containing Thermus aquaticus RNAP holoenzyme and promoter DNA that includes the full transcription bubble. The structures, combined with biochemical analyses, reveal key features supporting the formation and maintenance of the double-strand/single-strand DNA junction at the upstream edge of the -10 element where bubble formation initiates. The results also reveal RNAP interactions with duplex DNA just upstream of the -10 element and potential protein/DNA interactions that direct the DNA template strand into the RNAP active site. Addition of an RNA primer to yield a 4 base-pair post-translocated RNA:DNA hybrid mimics an initially transcribing complex at the point where steric clash initiates abortive initiation and σ(A) dissociation.
PubMed: 26349032
DOI: 10.7554/eLife.08504
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.6 Å)
Structure validation

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