Tags

Type your tag names separated by a space and hit enter

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.NS

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.

Authors+Show Affiliations

Alekshun MN
Center for Adaptation Genetics and Drug Resistance, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
Levy SB
No affiliation info available
Mealy TR
No affiliation info available
Seaton BA
No affiliation info available
Head JF
No affiliation info available

MeSH

Amino Acid MotifsAmino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayDNA-Binding ProteinsDimerizationDrug Resistance, MicrobialDrug Resistance, MultipleEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsRepressor ProteinsSalicylatesSequence Alignment

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

11473263

Citation

Alekshun, M N., et al. "The Crystal Structure of MarR, a Regulator of Multiple Antibiotic Resistance, at 2.3 a Resolution." Nature Structural Biology, vol. 8, no. 8, 2001, pp. 710-4.
Alekshun MN, Levy SB, Mealy TR, et al. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Nat Struct Biol. 2001;8(8):710-4.
Alekshun, M. N., Levy, S. B., Mealy, T. R., Seaton, B. A., & Head, J. F. (2001). The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Nature Structural Biology, 8(8), 710-4.
Alekshun MN, et al. The Crystal Structure of MarR, a Regulator of Multiple Antibiotic Resistance, at 2.3 a Resolution. Nat Struct Biol. 2001;8(8):710-4. PubMed PMID: 11473263.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. AU - Alekshun,M N, AU - Levy,S B, AU - Mealy,T R, AU - Seaton,B A, AU - Head,J F, PY - 2001/7/27/pubmed PY - 2001/8/17/medline PY - 2001/7/27/entrez SP - 710 EP - 4 JF - Nature structural biology JO - Nat Struct Biol VL - 8 IS - 8 N2 - 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. SN - 1072-8368 UR - https://www.unboundmedicine.com/medline/citation/11473263/The_crystal_structure_of_MarR_a_regulator_of_multiple_antibiotic_resistance_at_2_3_A_resolution_ L2 - https://imexcentral.org/icentral/imex/rec/IM-23521 DB - PRIME DP - Unbound Medicine ER -