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1tfi

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|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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'''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'''
'''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'''
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[[Category: Weiss, M A.]]
[[Category: Weiss, M A.]]
[[Category: Yoon, H S.]]
[[Category: Yoon, H S.]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:53:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:20 2008''
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Revision as of 06:53, 3 May 2008

Template:STRUCTURE 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


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 Page seeded by OCA on Sat May 3 09:53:28 2008

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