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Titolo:
A MODEL FOR THE LEXA REPRESSOR DNA COMPLEX
Autore:
KNEGTEL RMA; FOGH RH; OTTLEBEN G; RUTERJANS H; DUMOULIN P; SCHNARR M; BOELENS R; KAPTEIN R;
Indirizzi:
UNIV UTRECHT,BIJVOET CTR BIOMOLEC RES,PADUALAAN 8 3584 CH UTRECHT NETHERLANDS UNIV UTRECHT,BIJVOET CTR BIOMOLEC RES 3584 CH UTRECHT NETHERLANDS UNIV FRANKFURT,INST BIOPHYS CHEM W-6000 FRANKFURT 70 GERMANY CNRS,INST BIOL MOLEC & CELLULAIRE F-67084 STRASBOURG FRANCE
Titolo Testata:
Proteins
fascicolo: 3, volume: 21, anno: 1995,
pagine: 226 - 236
SICI:
0887-3585(1995)21:3<226:AMFTLR>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-TERMINAL DOMAIN; ESCHERICHIA-COLI; BINDING DOMAIN; CRYSTAL-STRUCTURE; OPERATOR DNA; PROTEIN; MOTIF; GENE; RECOGNITION;
Keywords:
DOCKING; MONTE CARLO; LEXA REPRESSOR; DNA BINDING DOMAIN; PROTEIN-DNA INTERACTION; SOLUTION STRUCTURE; MOLECULAR RECOGNITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
R.M.A. Knegtel et al., "A MODEL FOR THE LEXA REPRESSOR DNA COMPLEX", Proteins, 21(3), 1995, pp. 226-236

Abstract

A structural model for the interaction of the LexA repressor DNA binding domain (DBD) with operator DNA is derived by means of Monte Carlo docking. Protein-DNA complexes were generated by docking the LexA repressor DBD NMR solution structure onto both rigid and bent B-DNA structures while giving energy bonuses for contacts in agreement with experimental data. In the resulting complexes, helix III of the LexA repressor DBD is located in the major groove of the DNA and residues Asn-41, Glu-44, and Glu-45 form specific hydrogen bonds with bases of the CTGTDNA sequence. Ser-39, Ala-42, and Asn-41 are involved in a hydrophobic interaction with the methyl group of the first thymine base. Residues in the loop region connecting the two beta-sheet strands are involved in nonspecific contacts near the dyad axis of the operator. The contacts observed in the docked complexes cover the entire consensus CTGT half-site DNA operator, thus explaining the specificity of the LexA repressor for such sequences. In addition, a large number of nonspecificinteractions between protein and DNA is observed. The agreement between the derived model for the LexA repressor DBD/DNA complex and experimental biochemical results is discussed. (C) 1995 Wiley-Liss, Inc.

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Documento generato il 03/04/20 alle ore 20:19:57