1ENW
ELONGATION FACTOR TFIIS DOMAIN II
Summary for 1ENW
| Entry DOI | 10.2210/pdb1enw/pdb |
| Descriptor | TRANSCRIPTION ELONGATION FACTOR S-II (1 entity in total) |
| Functional Keywords | helix-bundle, transcription |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 12732.34 |
| Authors | Morin, P.E.,Awrey, D.E.,Edwards, A.M.,Arrowsmith, C.H. (deposition date: 2000-03-21, release date: 2000-04-12, Last modification date: 2024-05-22) |
| Primary citation | Morin, P.E.,Awrey, D.E.,Edwards, A.M.,Arrowsmith, C.H. Elongation factor TFIIS contains three structural domains: solution structure of domain II. Proc.Natl.Acad.Sci.USA, 93:10604-10608, 1996 Cited by PubMed Abstract: Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. Limited proteolytic digestion showed that yeast TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III) are required for transcription activity. The structure of domain III has been solved previously by using NMR spectroscopy. Here, we report the NMR-derived structure of domain II: a three-helix bundle built around a hydrophobic core composed largely of three tyrosines protruding from one face of the C-terminal helix. The arrangement of known inactivating mutations of TFIIS suggests that two surfaces of domain II are critical for transcription activity. PubMed: 8855225DOI: 10.1073/pnas.93.20.10604 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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