1tfi
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(New page: 200px<br /> <applet load="1tfi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfi" /> '''A NOVEL ZN FINGER MOTIF IN THE BASAL TRANSC...)
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Revision as of 17:17, 12 November 2007
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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
Overview
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.
About this Structure
1TFI is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Novel zinc finger motif in the basal transcriptional machinery: three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS., Qian X, Gozani SN, Yoon H, Jeon CJ, Agarwal K, Weiss MA, Biochemistry. 1993 Sep 28;32(38):9944-59. PMID:8399164
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