PDBsum entry: 1jbg

Transcription

PDB id: 1jbg

Contents

Protein chain

106 a.a. *

Waters ×16

* Residue conservation analysis

PDB id:

1jbg

Name:

Transcription

Title:

Crystal structure of mtan, the bacillus subtilis multidrug t activator, n-terminus

Structure:

Transcription activator of multidrug-efflux trans genes mta. Chain: a. Fragment: n-terminus (residues 1-109). Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.75Å R-factor: 0.228 R-free: 0.287

Authors:

M.H.Godsey,A.A.Neyfakh,R.G.Brennan

Key ref:

M.H.Godsey et al. (2001). Crystal structure of MtaN, a global multidrug transporter gene activator. J Biol Chem, 276, 47178-47184. PubMed id: 11581256 DOI: 10.1074/jbc.M105819200

Date:

04-Jun-01 Release date: 28-Nov-01

Protein chain

P71039  (MTA_BACSU) -  HTH-type transcriptional activator mta

Seq: 257 a.a.

Struc: 106 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: regulation of transcription, DNA-dependent (1 term)
• Biochemical function: nucleotide binding (2 terms)

DOI no: 10.1074/jbc.M105819200

J Biol Chem 276:47178-47184 (2001)

PubMed id: 11581256

Crystal structure of MtaN, a global multidrug transporter gene activator.

M.H.Godsey, N.N.Baranova, A.A.Neyfakh, R.G.Brennan.

ABSTRACT

MtaN (Multidrug Transporter Activation, N terminus) is a constitutive, transcriptionally active 109-residue truncation mutant, which contains only the N-terminal DNA-binding and dimerization domains of MerR family member Mta. The 2.75 A resolution crystal structure of apo-MtaN reveals a winged helix-turn-helix protein with a protruding 8-turn helix (alpha5) that is involved in dimerization by the formation of an antiparallel coiled-coil. The hydrophobic core and helices alpha1 through alpha4 are structurally homologous to MerR family member BmrR bound to DNA, whereas one wing (Wing 1) is shifted. Differences between the orientation of alpha5 with respect to the core and the revolution of the antiparallel coiled-coil lead to significantly altered conformations of MtaN and BmrR dimers. These shifts result in a conformation of MtaN that appears to be incompatible with the transcription activation mechanism of BmrR and suggest that additional DNA-induced structural changes are necessary.

Selected figure(s)

Figure 1.
Fig. 1. A stereo view of the overall architecture of MtaN. Every tenth residue is labeled.

Figure 4.
Fig. 4. A schematic diagram of the antiparallel coiled-coil of MtaN. Intersubunit salt bridges between the a and e positions are depicted by gray lines. Residues at the a and d positions form the hydrophobic core of the interacting helices.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 47178-47184) copyright 2001.

Figures were selected by an automated process.