4G7O
Crystal structure of Thermus thermophilus transcription initiation complex containing 2 nt of RNA
Summary for 4G7O
Entry DOI | 10.2210/pdb4g7o/pdb |
Related | 4G7H 4G7Z |
Descriptor | DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (11 entities in total) |
Functional Keywords | protein-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 source | Thermus thermophilus More |
Total number of polymer chains | 18 |
Total formula weight | 889143.22 |
Authors | Zhang, Y.,Ebright, R.H. (deposition date: 2012-07-20, release date: 2012-10-31, Last modification date: 2023-09-13) |
Primary citation | Zhang, 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: 23086998DOI: 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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