1BL0

MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN (MARA)/DNA COMPLEX

Summary for 1BL0

• Entry DOI: 10.2210/pdb1bl0/pdb
• Descriptor: DNA (5'-D(*GP*GP*GP*GP*AP*TP*TP*TP*AP*GP*CP*AP*AP*AP*AP*CP*GP*TP*GP*GP*CP*AP* TP*C)-3'), DNA (5'-D(*CP*CP*GP*AP*TP*GP*CP*CP*AP*CP*GP*TP*TP*TP*TP*GP*CP*TP*AP*AP*AP*TP* CP*C)-3'), PROTEIN (MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN), ... (4 entities in total)
• Functional Keywords: transcriptional activator; a bipartite helix-turn-helix protein, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 30181.03

Authors

Davies, S.,Rhee, R.G.,Martin, J.L.,Rosner, D.R. (deposition date: 1998-07-22, release date: 1998-09-02, Last modification date: 2024-02-07)

Primary citation

Rhee, S.,Martin, R.G.,Rosner, J.L.,Davies, D.R.
A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator.
Proc.Natl.Acad.Sci.USA, 95:10413-10418, 1998

PubMed 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.

PubMed: 9724717
DOI: 10.1073/pnas.95.18.10413

Experimental method

X-RAY DIFFRACTION (2.3 Å)