Structural highlights
Function
[MARR_ECOLI] Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
MarR is a regulator of multiple antibiotic resistance in Escherichia coli. It is the prototypical member of the MarR family of regulatory proteins found in bacteria and archaea that play important roles in the development of antibiotic resistance, a global health problem. Here we describe the crystal structure of the MarR protein, determined at a resolution of 2.3 A. This is the first reported crystal structure of a member of this newly-described protein family. The structure shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.
The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution.,Alekshun MN, Levy SB, Mealy TR, Seaton BA, Head JF Nat Struct Biol. 2001 Aug;8(8):710-4. PMID:11473263[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alekshun MN, Levy SB, Mealy TR, Seaton BA, Head JF. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Nat Struct Biol. 2001 Aug;8(8):710-4. PMID:11473263 doi:10.1038/90429
