PDBsum entry 4zjo

Transport protein

PDB id: 4zjo

Contents

Protein chains

(+ 0 more) 1042 a.a.

Ligands

ERY ×2

LMT ×8

Metals

_NI ×3

PDB id:

4zjo

Name:

Transport protein

Title:

Crystal structure of acrb triple mutant in complex with antibiotic in p21 space group

Structure:

Multidrug efflux pump subunit acrb. Chain: a, b, c, d, e, f. Synonym: acrab-tolc multidrug efflux pump subunit acrb,acridine resistance protein b. Engineered: yes

Source:

Escherichia coli str. K-12 substr. Mg1655. Organism_taxid: 511145. Gene: acrb, acre, b0462, jw0451. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

3.60Å R-factor: 0.241 R-free: 0.307

Authors:

A.Ababou,V.Koronakis

Key ref:

A.Ababou and V.Koronakis (2016). Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate. Plos One, 11, e0159154. PubMed id: 27403665 DOI: 10.1371/journal.pone.0159154

Date:

29-Apr-15 Release date: 27-Jul-16

Protein chains

P31224  (ACRB_ECOLI) -  Multidrug efflux pump subunit AcrB from Escherichia coli (strain K12)

Seq: 1049 a.a.

Struc: 1042 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1371/journal.pone.0159154

Plos One 11:e0159154 (2016)

PubMed id: 27403665

Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate.

A.Ababou, V.Koronakis.

ABSTRACT

Gram-negative bacteria such as E. coli use tripartite efflux pumps such as AcrAB-TolC to expel antibiotics and noxious compounds. A key feature of the inner membrane transporter component, AcrB, is a short stretch of residues known as the gate/switch loop that divides the proximal and distal substrate binding pockets. Amino acid substitutions of the gate loop are known to decrease antibiotic resistance conferred by AcrB. Here we present two new AcrB gate loop variants, the first stripped of its bulky side chains, and a second in which the gate loop is removed entirely. By determining the crystal structures of the variant AcrB proteins in the presence and absence of erythromycin and assessing their ability to confer erythromycin tolerance, we demonstrate that the gate loop is important for AcrB export activity but is not required for erythromycin binding.