1D8K
SOLUTION STRUCTURE OF THE CENTRAL CORE DOMAIN OF TFIIE BETA
Summary for 1D8K
| Entry DOI | 10.2210/pdb1d8k/pdb |
| Related | 1D8J |
| Descriptor | GENERAL TRANSCRIPTION FACTOR TFIIE-BETA (1 entity in total) |
| Functional Keywords | winged helix-turn-helix, riken structural genomics/proteomics initiative, rsgi, structural genomics, gene regulation |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P29084 |
| Total number of polymer chains | 1 |
| Total formula weight | 9287.70 |
| Authors | Okuda, M.,Watanabe, Y.,Okamura, H.,Hanaoka, F.,Ohkuma, Y.,Nishimura, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1999-10-25, release date: 2000-04-26, Last modification date: 2024-05-22) |
| Primary citation | Okuda, M.,Watanabe, Y.,Okamura, H.,Hanaoka, F.,Ohkuma, Y.,Nishimura, Y. Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface. EMBO J., 19:1346-1356, 2000 Cited by PubMed Abstract: Human general transcription factor TFIIE consists of two subunits, TFIIEalpha and TFIIEbeta. Recently, TFIIEbeta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. Here, the central core domain of human TFIIEbeta (TFIIEbetac) has been identified by a limited proteolysis. This solution structure has been determined by NMR. It consists of three helices with a beta hairpin at the C-terminus, resembling the winged helix proteins. However, TFIIEbetac shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow. A model will be proposed that TFIIE stabilizes the preinitiation complex by binding not only to the general transcription factors together with RNA polymerase II but also to the promoter DNA, where double-stranded DNA starts to open to be single-stranded upon activation of the preinitiation complex. PubMed: 10716934DOI: 10.1093/emboj/19.6.1346 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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