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1JGS

Multiple Antibiotic Resistance Repressor, MarR

Summary for 1JGS
Entry DOI10.2210/pdb1jgs/pdb
DescriptorMULTIPLE ANTIBIOTIC RESISTANCE PROTEIN MARR, 2-HYDROXYBENZOIC ACID (2 entities in total)
Functional Keywordstranscription regulation, dna-binding, repressor, antibiotic resistance, transcription
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight15712.54
Authors
Alekshun, M.N.,Levy, S.B.,Mealy, T.R.,Seaton, B.A.,Head, J.F. (deposition date: 2001-06-26, release date: 2001-12-28, Last modification date: 2024-02-07)
Primary citationAlekshun, M.N.,Levy, S.B.,Mealy, T.R.,Seaton, B.A.,Head, J.F.
The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution.
Nat.Struct.Biol., 8:710-714, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11473263
DOI: 10.1038/90429
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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