A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator

Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10413-8. doi: 10.1073/pnas.95.18.10413.

Abstract

A crystal structure for a member of the AraC prokaryotic transcriptional activator family, MarA, in complex with its cognate DNA-binding site is described. MarA consists of two similar subdomains, each containing a helix-turn-helix DNA-binding motif. The two recognition helices of the motifs are inserted into adjacent major groove segments on the same face of the DNA but are separated by only 27 A thereby bending the DNA by approximately 35 degrees. Extensive interactions between the recognition helices and the DNA major groove provide the sequence specificity.

MeSH terms

  • Amino Acid Sequence
  • AraC Transcription Factor
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Crystallography, X-Ray
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli Proteins*
  • Hydrogen Bonding
  • Molecular Sequence Data
  • Protein Conformation
  • Repressor Proteins / chemistry
  • Repressor Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism*
  • Transcription Factors*

Substances

  • AraC Transcription Factor
  • AraC protein, E coli
  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • MarA protein, E coli
  • Repressor Proteins
  • Trans-Activators
  • Transcription Factors
  • DNA

Associated data

  • PDB/1BL0