1VD4
Solution structure of the zinc finger domain of TFIIE alpha
Summary for 1VD4
| Entry DOI | 10.2210/pdb1vd4/pdb |
| Related | 1D8J 1D8K |
| Descriptor | Transcription initiation factor IIE, alpha subunit, ZINC ION (2 entities in total) |
| Functional Keywords | zinc finger, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P29083 |
| Total number of polymer chains | 1 |
| Total formula weight | 7171.23 |
| Authors | Okuda, M.,Tanaka, A.,Arai, Y.,Satoh, M.,Okamura, H.,Nagadoi, A.,Hanaoka, F.,Ohkuma, Y.,Nishimura, Y. (deposition date: 2004-03-18, release date: 2004-10-05, Last modification date: 2023-12-27) |
| Primary citation | Okuda, M.,Tanaka, A.,Arai, Y.,Satoh, M.,Okamura, H.,Nagadoi, A.,Hanaoka, F.,Ohkuma, Y.,Nishimura, Y. A novel zinc finger structure in the large subunit of human general transcription factor TFIIE. J.Biol.Chem., 279:51395-51403, 2004 Cited by PubMed Abstract: The zinc finger domain in the large subunit of TFIIE (TFIIEalpha) is phylogenetically conserved and is essential for transcription. Here, we determined the solution structure of this domain by using NMR. It consisted of one alpha-helix and five beta-strands, showing novel features distinct from previously determined zinc-binding structures. We created point mutants of TFIIEalpha in this domain and examined their binding abilities to other general transcription factors as well as their transcription activities. Four Zn(2+)-ligand mutants, in which each of cysteine residues at positions 129, 132, 154, and 157 was replaced by alanine, possessed no transcription activities on a linearized template, whereas, on a supercoiled template, interesting functional asymmetry was observed: although the C-terminal two mutants abolished transcription activity (<5%), the N-terminal two mutants retained about 20% activities. The N-terminal two mutants bound stronger to the small subunit of TFIIF than the wild type and the C-terminal two mutants were impaired in their binding abilities to the XPB subunits of TFIIH. These suggest that the structural integrity of the zinc finger domain is essential for the TFIIE function, particularly in the transition from the transcription initiation to elongation and the conformational tuning of this domain for appropriate positioning of TFIIF, TFIIH, and polymerase II would be needed depending on the situation and timing. PubMed: 15385556DOI: 10.1074/jbc.M404722200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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