1tfi
From Proteopedia
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| - | [[Image:1tfi.jpg|left|200px]] | + | [[Image:1tfi.jpg|left|200px]] | 
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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''' | + |  {{Structure | 
| + | |PDB= 1tfi |SIZE=350|CAPTION= <scene name='initialview01'>1tfi</scene> | ||
| + | |SITE=  | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY=  | ||
| + | |GENE=  | ||
| + | }} | ||
| + | |||
| + | '''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== | ==Overview== | ||
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| ==About this Structure== | ==About this Structure== | ||
| - | 1TFI is a [ | + | 1TFI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFI OCA].  | 
| ==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8399164 8399164] | 
| [[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| [[Category: Single protein]] | [[Category: Single protein]] | ||
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| [[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:43 2008'' | 
Revision as of 12:17, 20 March 2008
 
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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. 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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