PDBsum entry 2mrn

DNA binding protein

PDB id: 2mrn

Contents

Protein chains

67 a.a.

PDB id:

2mrn

Name:

DNA binding protein

Title:

Structure of truncated ecmaze

Structure:

Antitoxin maze. Chain: a, b. Fragment: DNA-binding domain (unp residues 2-50). Engineered: yes

Source:

Escherichia coli k-12. Organism_taxid: 83333. Gene: b2783, bn896_2518, chpai, chpr, jw2754, maze. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

V.Zorzini,L.Buts,R.Loris,N.A.J.Van Nuland

Key ref:

V.Zorzini et al. (2015). Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding. Nucleic Acids Res, 43, 1241-1256. PubMed id: 25564525 DOI: 10.1093/nar/gku1352

Date:

12-Jul-14 Release date: 04-Feb-15

Protein chains

P0AE72  (MAZE_ECOLI) -  Antitoxin MazE from Escherichia coli (strain K12)

Seq: 82 a.a.

Struc: 67 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gku1352

Nucleic Acids Res 43:1241-1256 (2015)

PubMed id: 25564525

Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding.

V.Zorzini, L.Buts, E.Schrank, Y.G.Sterckx, M.Respondek, H.Engelberg-Kulka, R.Loris, K.Zangger, N.A.van Nuland.

ABSTRACT

Toxin-antitoxin (TA) modules are pairs of genes essential for bacterial regulation upon environmental stresses. The mazEF module encodes the MazF toxin and its cognate MazE antitoxin. The highly dynamic MazE possesses an N-terminal DNA binding domain through which it can negatively regulate its own promoter. Despite being one of the first TA systems studied, transcriptional regulation of Escherichia coli mazEF remains poorly understood. This paper presents the solution structure of C-terminal truncated E. coli MazE and a MazE-DNA model with a DNA palindrome sequence ∼10 bp upstream of the mazEF promoter. The work has led to a transcription regulator-DNA model, which has remained elusive thus far in the E. coli toxin-antitoxin family. Multiple complementary techniques including NMR, SAXS and ITC show that the long intrinsically disordered C-termini in MazE, required for MazF neutralization, does not affect the interactions between the antitoxin and its operator. Rather, the MazE C-terminus plays an important role in the MazF binding, which was found to increase the MazE affinity for the palindromic single site operator.