3K7A
Crystal Structure of an RNA polymerase II-TFIIB complex
Summary for 3K7A
| Entry DOI | 10.2210/pdb3k7a/pdb |
| Descriptor | DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC4, Transcription initiation factor IIB, ... (12 entities in total) |
| Functional Keywords | rna polymerase ii, tfiib, transcription, dna-binding, dna-directed rna polymerase, isopeptide bond, magnesium, metal-binding, nucleotidyltransferase, nucleus, phosphoprotein, transferase, zinc-finger, dna damage, dna repair, transcription regulation |
| Biological source | Saccharomyces cerevisiae (yeast) More |
| Cellular location | Nucleus: P04050 P29055 P08518 P16370 P20434 P20436 P27999 P38902 Nucleus, nucleolus: P40422 P22139 Cytoplasm: P20435 |
| Total number of polymer chains | 11 |
| Total formula weight | 508472.00 |
| Authors | Liu, X.,Bushnell, D.A.,Wang, D.,Calero, G.,Kornberg, R.D. (deposition date: 2009-10-12, release date: 2009-11-24, Last modification date: 2024-11-27) |
| Primary citation | Liu, X.,Bushnell, D.A.,Wang, D.,Calero, G.,Kornberg, R.D. Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism. Science, 327:206-209, 2010 Cited by PubMed Abstract: Previous x-ray crystal structures have given insight into the mechanism of transcription and the role of general transcription factors in the initiation of the process. A structure of an RNA polymerase II-general transcription factor TFIIB complex at 4.5 angstrom resolution revealed the amino-terminal region of TFIIB, including a loop termed the "B finger," reaching into the active center of the polymerase where it may interact with both DNA and RNA, but this structure showed little of the carboxyl-terminal region. A new crystal structure of the same complex at 3.8 angstrom resolution obtained under different solution conditions is complementary with the previous one, revealing the carboxyl-terminal region of TFIIB, located above the polymerase active center cleft, but showing none of the B finger. In the new structure, the linker between the amino- and carboxyl-terminal regions can also be seen, snaking down from above the cleft toward the active center. The two structures, taken together with others previously obtained, dispel long-standing mysteries of the transcription initiation process. PubMed: 19965383DOI: 10.1126/science.1182015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.8 Å) |
Structure validation
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