PDBsum entry: 1jgs

Transcription

PDB id: 1jgs

Contents

Protein chain

138 a.a. *

Ligands

SAL ×2

* Residue conservation analysis

PDB id:

1jgs

Name:

Transcription

Title:

Multiple antibiotic resistance repressor, marr

Structure:

Multiple antibiotic resistance protein marr. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.30Å R-factor: 0.247 R-free: 0.287

Authors:

M.N.Alekshun,S.B.Levy,T.R.Mealy,B.A.Seaton,J.F.Head

Key ref:

M.N.Alekshun et al. (2001). The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Nat Struct Biol, 8, 710-714. PubMed id: 11473263 DOI: 10.1038/90429

Date:

26-Jun-01 Release date: 28-Dec-01

Protein chain

P27245  (MARR_ECOLI) -  Multiple antibiotic resistance protein marR

Seq: 144 a.a.

Struc: 138 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)
• Biological process: response to antibiotic (3 terms)
• Biochemical function: DNA binding (2 terms)

DOI no: 10.1038/90429

Nat Struct Biol 8:710-714 (2001)

PubMed id: 11473263

The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution.

M.N.Alekshun, S.B.Levy, T.R.Mealy, B.A.Seaton, J.F.Head.

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.

Selected figure(s)

Figure 1.
Figure 1. The structure of MarR. a, Sequence alignment of MarR with representative members of the MarR family. The MarR secondary structure elements were identified in the present structure and are illustrated as tubes for -helices ( ) and arrows for -sheets ( ); the single wing region (W1) in MarR is indicated. Numbering is according to the MarR primary sequence. Residues that are identical in all homologs are colored in red, highly conserved amino acids in yellow and moderately conserved residues in blue. Residues marked with a 'plus sign' form the hydrophobic core of the N-/C-terminal domain of MarR, and those denoted with an 'asterisk' form the hydrophobic core of the individual DNA-binding domains. The proteins used for the alignment were from the following organisms: MarR, E. coli; MprA (EmrR), E. coli; MexR, P. aeruginosa; YS87, Mycobacterium tuberculosis; SlyA, S. typhimurium; PecS, Erwinia chrysanthemi; and CinR, Butyrivibrio fibrisolvens. This figure was prepared using ALSCRIPT35. b, Ribbon representation of the cocrystal structure of the MarR dimer viewed with the subunit two-fold axis near vertical. The secondary structure elements of one subunit are colored according to the scheme used in (a). The first six N-terminal residues of MarR are disordered and not included in the structure. c, Electrostatic surface representation of the MarR dimer. d, A C trace of a single MarR subunit in stereo representation. The diagrams in (b -d) are all viewed in the same orientation and were all prepared using Swiss PDB Viewer36; (b) was rendered with POVRAY37.

Figure 2.
Figure 2. Regions involved in protein -protein interactions. a, The core of the N-/C- terminal domain is represented by a surface (red) around the van der Waals radii of the side chain atoms only of the hydrophobic core residues (indicated by a 'plus sign' in Fig. 1a). The main chain and other residues of the domain are shown in yellow for one subunit and blue for the other. Helices leading to and from the domain are shown in ribbon representation. b, Interactions between the DNA-binding domains of the dimer are observed only in the region of the Arg 73 -Asp 67' salt bridges. The proximity of the two salicylate-binding sites per monomer is also shown. This stereo view is coincident with the two-fold rotation axis of the dimer. Electron density shown is a 2F[O] - F[C] map contoured at 1 .

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2001, 8, 710-714) copyright 2001.