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Titolo:
SOLUTION STRUCTURE OF THE FIRST 3 ZINC FINGERS OF TFIIIA BOUND TO THECOGNATE DNA-SEQUENCE - DETERMINANTS OF AFFINITY AND SEQUENCE SPECIFICITY
Autore:
WUTTKE DS; FOSTER MP; CASE DA; GOTTESFELD JM; WRIGHT PE;
Indirizzi:
SCRIPPS CLIN & RES INST,DEPT BIOL MOL,10550 N TORREY,PINES RD LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,DEPT BIOL MOL LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,SKAGGS INST CHEM BIOL LA JOLLA CA 92037
Titolo Testata:
Journal of Molecular Biology
fascicolo: 1, volume: 273, anno: 1997,
pagine: 183 - 206
SICI:
0022-2836(1997)273:1<183:SSOTF3>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR-IIIA; 5S RNA GENE; INTERNAL CONTROL REGION; NUCLEAR-MAGNETIC-RESONANCE; DIRECTS SPECIFIC INITIATION; PROTEIN-PEPTIDE COMPLEX; CRYSTAL-STRUCTURE; J-COUPLINGS; FUNCTIONAL DOMAINS; BINDING DOMAINS;
Keywords:
TFIIIA; ZINC FINGER; PROTEIN-DNA RECOGNITION; NMR STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
85
Recensione:
Indirizzi per estratti:
Citazione:
D.S. Wuttke et al., "SOLUTION STRUCTURE OF THE FIRST 3 ZINC FINGERS OF TFIIIA BOUND TO THECOGNATE DNA-SEQUENCE - DETERMINANTS OF AFFINITY AND SEQUENCE SPECIFICITY", Journal of Molecular Biology, 273(1), 1997, pp. 183-206

Abstract

The high resolution solution structure of a protein containing the three amino-terminal zinc fingers of Xenopus laevis transcription factorIIIA (TFIIIA) bound to its cognate DNA duplex was determined by nuclear magnetic resonance spectroscopy. The protein, which is designated zf1-3, binds with all three fingers in the DNA major groove, with a number of amino acids making base-specific contacts. The DNA structure isclose to B-form. Although the mode of interaction of ef1-3 with DNA is similar to that of zif268 and other structurally characterized zinc finger complexes, the TFIIIA complex exhibits several novel features. Each zinc finger contacts four to five base-pairs and the repertoire of known base contact residues is extended to include a tryptophan at position +2 of the helix (finger 1) and arginine at position +10 (finger 3). Sequence-specific base contacts are made over virtually the entire length of the finger 3 helix. Lysine and histidine side-chains involved in base recognition are dynamically disordered in the solution structure; in the case of lysine, in particular, this could significantly decrease the entropic cost of DNA binding. The TGEKP(N) linker sequences, which are highly flexible in the unbound protein, adopt ordered conformations on DNA binding. The linkers appear to play an active structural role in stabilization of the protein-DNA complex. Substantial protein-protein contact surfaces are formed between adjacent fingers. As a consequence of these protein-protein interactions, the orientation of finger 1 in the major groove differs from that of the other fingers. Contributions to high affinity binding by zf1-3 come from both direct protein-DNA contacts and from indirect protein-protein interactions associated with structural organization of the linkers and formationof well-packed interfaces between adjacent zinc fingers in the DNA complex. The structures provide a molecular level explanation for the large body of footprinting and mutagenesis data available for the TFIIIA-DNA complex. (C) 1997 Academic Press Limited.

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Documento generato il 28/09/20 alle ore 13:18:44