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4G7O

Crystal structure of Thermus thermophilus transcription initiation complex containing 2 nt of RNA

Summary for 4G7O
Entry DOI10.2210/pdb4g7o/pdb
Related4G7H 4G7Z
DescriptorDNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (11 entities in total)
Functional Keywordsprotein-dna complex, transcription initiation complex, rnap-promoter complex, rnap-promoter open complex, open complex, rpo, rna polymerase, transcription initiation, transcription initiation factor sigma a, promoter dna, nucleoid, transcription, transferase-dna complex, transferase/dna
Biological sourceThermus thermophilus
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Total number of polymer chains18
Total formula weight889143.22
Authors
Zhang, Y.,Ebright, R.H. (deposition date: 2012-07-20, release date: 2012-10-31, Last modification date: 2023-09-13)
Primary citationZhang, Y.,Feng, Y.,Chatterjee, S.,Tuske, S.,Ho, M.X.,Arnold, E.,Ebright, R.H.
Structural basis of transcription initiation.
Science, 338:1076-1080, 2012
Cited by
PubMed Abstract: During transcription initiation, RNA polymerase (RNAP) binds and unwinds promoter DNA to form an RNAP-promoter open complex. We have determined crystal structures at 2.9 and 3.0 Å resolution of functional transcription initiation complexes comprising Thermus thermophilus RNA polymerase, σ(A), and a promoter DNA fragment corresponding to the transcription bubble and downstream double-stranded DNA of the RNAP-promoter open complex. The structures show that σ recognizes the -10 element and discriminator element through interactions that include the unstacking and insertion into pockets of three DNA bases and that RNAP recognizes the -4/+2 region through interactions that include the unstacking and insertion into a pocket of the +2 base. The structures further show that interactions between σ and template-strand single-stranded DNA (ssDNA) preorganize template-strand ssDNA to engage the RNAP active center.
PubMed: 23086998
DOI: 10.1126/science.1227786
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.993 Å)
Structure validation

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