1tfi
From Proteopedia
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|PDB= 1tfi |SIZE=350|CAPTION= <scene name='initialview01'>1tfi</scene> | |PDB= 1tfi |SIZE=350|CAPTION= <scene name='initialview01'>1tfi</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfi OCA], [http://www.ebi.ac.uk/pdbsum/1tfi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfi RCSB]</span> | ||
}} | }} | ||
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[[Category: Weiss, M A.]] | [[Category: Weiss, M A.]] | ||
[[Category: Yoon, H S.]] | [[Category: Yoon, H S.]] | ||
| - | [[Category: ZN]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:20 2008'' |
Revision as of 20:55, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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