1TFI
A NOVEL ZN FINGER MOTIF IN THE BASAL TRANSCRIPTIONAL MACHINERY: THREE-DIMENSIONAL NMR STUDIES OF THE NUCLEIC-ACID BINDING DOMAIN OF TRANSCRIPTIONAL ELONGATION FACTOR TFIIS
Summary for 1TFI
| Entry DOI | 10.2210/pdb1tfi/pdb |
| Descriptor | TRANSCRIPTIONAL ELONGATION FACTOR SII, ZINC ION (2 entities in total) |
| Functional Keywords | transcription regulation |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P23193 |
| Total number of polymer chains | 1 |
| Total formula weight | 5732.91 |
| Authors | Qian, X.,Gozani, S.,Yoon, H.S.,Jeon, C.J.,Agarwal, K.,Weiss, M.A. (deposition date: 1993-04-27, release date: 1993-10-31, Last modification date: 2024-05-22) |
| Primary citation | Qian, X.,Gozani, S.N.,Yoon, H.,Jeon, C.J.,Agarwal, K.,Weiss, M.A. Novel zinc finger motif in the basal transcriptional machinery: three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS. Biochemistry, 32:9944-9959, 1993 Cited by PubMed Abstract: Transcriptional elongation provides a key control point in the regulation of eukaryotic gene expression. Here we describe homonuclear and 15N-heteronuclear 3D NMR studies of the nucleic acid binding domain of human transcriptional elongation factor TFIIS. This domain contains a Cys4 Zn(2+)-binding site with no homology to previously characterized Cys4, Cys6, or Cys2-His2 Zn fingers. Complete 1H and 15N NMR resonance assignment of a 50-residue TFIIS peptide-Zn2+ complex is obtained. Its solution structure, as determined by distance geometry/simulated annealing (DG/SA) calculations, exhibits a novel three-stranded antiparallel beta-sheet (designated the Zn ribbon). Analogous sequence motifs occur in a wide class of proteins involved in RNA or DNA transactions, including human basal transcriptional initiation factor TFIIE. A three-dimensional model of the TFIIE Cys4 domain is obtained by DG-based homology modeling. The role of the TFIIS Zn ribbon in the control of eukaryotic transcriptional elongation is discussed. PubMed: 8399164DOI: 10.1021/bi00089a010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
