PDBsum entry 3vod

Transcription

PDB id: 3vod

Contents

Protein chains

136 a.a.

PDB id:

3vod

Name:

Transcription

Title:

Crystal structure of mutant marr c80s from e.Coli

Structure:

Multiple antibiotic resistance protein marr. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b1530, cfxb, inar, jw5248, marr, soxq. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.60Å R-factor: 0.257 R-free: 0.281

Authors:

H.Lou,R.Zhu,Z.Hao

Key ref:

Z.Hao et al. (2014). The multiple antibiotic resistance regulator MarR is a copper sensor in Escherichia coli. Nat Chem Biol, 10, 21-28. PubMed id: 24185215 DOI: 10.1038/nchembio.1380

Date:

21-Jan-12 Release date: 06-Mar-13

Protein chains

P27245  (MARR_ECOLI) -  Multiple antibiotic resistance protein MarR from Escherichia coli (strain K12)

Seq: 144 a.a.

Struc: 136 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nchembio.1380

Nat Chem Biol 10:21-28 (2014)

PubMed id: 24185215

The multiple antibiotic resistance regulator MarR is a copper sensor in Escherichia coli.

Z.Hao, H.Lou, R.Zhu, J.Zhu, D.Zhang, B.S.Zhao, S.Zeng, X.Chen, J.Chan, C.He, P.R.Chen.

ABSTRACT

The widely conserved multiple antibiotic resistance regulator (MarR) family of transcription factors modulates bacterial detoxification in response to diverse antibiotics, toxic chemicals or both. The natural inducer for Escherichia coli MarR, the prototypical transcription repressor within this family, remains unknown. Here we show that copper signaling potentiates MarR derepression in E. coli. Copper(II) oxidizes a cysteine residue (Cys80) on MarR to generate disulfide bonds between two MarR dimers, thereby inducing tetramer formation and the dissociation of MarR from its cognate promoter DNA. We further discovered that salicylate, a putative MarR inducer, and the clinically important bactericidal antibiotics norfloxacin and ampicillin all stimulate intracellular copper elevation, most likely through oxidative impairment of copper-dependent envelope proteins, including NADH dehydrogenase-2. This membrane-associated copper oxidation and liberation process derepresses MarR, causing increased bacterial antibiotic resistance. Our study reveals that this bacterial transcription regulator senses copper(II) as a natural signal to cope with stress caused by antibiotics or the environment.