A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
Authors:
- 1 September 1998
- journal article
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 95 (18) , 10413-10418
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 Å thereby bending the DNA by ≈35°. Extensive interactions between the recognition helices and the DNA major groove provide the sequence specificity.Keywords
This publication has 31 references indexed in Scilit:
- [32] Collaborative computational project, number 4: Providing programs for protein crystallography1997
- [20] Processing of X-ray diffraction data collected in oscillation mode1997
- Structural Classification of HTH DNA-binding Domains and Protein – DNA Interaction ModesJournal of Molecular Biology, 1996
- The Crystal Structure of the DNA-Binding Domain of Yeast RAP1 in Complex with Telomeric DNACell, 1996
- New parameters for the refinement of nucleic acid-containing structuresActa Crystallographica Section D Structural Biology, 1996
- Protein Structure Comparison by Alignment of Distance MatricesJournal of Molecular Biology, 1993
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- TRANSCRIPTION FACTORS: Structural Families and Principles of DNA RecognitionAnnual Review of Biochemistry, 1992
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- REGULATION: POSITIVE CONTROLAnnual Review of Genetics, 1974