Crystallisation and preliminary X-ray analysis of two variants of the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex

Yann Sterckx; Sarah Haesaerts; Laurence Van Melderen; Remy Loris

Crystallisation and preliminary X-ray analysis of two variants of the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex

Yann Sterckx, Sarah Haesaerts, Laurence Van Melderen, Remy Loris

Research output: Contribution to journal › Article

Abstract

The paaR2-paaA2-parE2 operon is a three-component toxin-antitoxin (TA) module encoded in the genome of the human pathogen E. coli O157. The toxin (ParE2) and antitoxin (PaaA2) interact to form a non-toxic antitoxin-toxin complex. In this paper, the crystallisation and preliminary characterisation of two variants of the PaaA2-ParE2 antitoxin-toxin complex are described. Seleno-methionine derivative crystals of the full-length PaaA2-ParE2 antitoxin-toxin complex diffract to 2.8 Å and belong to space group P41212 (or P43212) with unit cell parameters a = b = 90.5 Å, c = 412.3 Å. In contrast, ParE2 and PaaA213-63, a truncated form of PaaA2 in which the first 12 N-terminal residues of the antitoxin have been deleted, form a hetero-dimer as evidenced by analytical gel filtration, dynamic light scattering, and small-angle X-ray scattering. Crystals of the PaaA213-63-ParE2 complex diffract to 2.7 Å and belong to space group P6122 (or P6522) with unit cell parameters a = b = 91.6 Å, c = 185.6 Å.

Original language	English
Pages (from-to)	1284-1291
Number of pages	8
Journal	Acta Crystallogr F Struct Biol Commun
Volume	70
Publication status	Published - 2014

Keywords

structural biology
bacterial stress response
X-ray crystallography
toxin-antitoxin module
persistence

1 Active
3 Finished

SRP13: Strategic Research Programme: Structure and dynamics of macromolecular complexes in health and disease
Steyaert, J., Remaut, H. K., Loris, R., Efremov, R., Steyaert, J., Loris, R. & Remaut, H. K.
1/11/12 → 31/10/22
Project: Fundamental
FWOAL699: ESRF and DUBBLE: Synchrotron X-rays for revealing the structure and function of molecules and materials
Loris, R., Remaut, H. K., Goderis, B., Janssens, K., Kirschhock, C. E. A., Van Bael, M., Poelman, D., Temst, K., Adriaens, A. & Laszlo, V.
1/01/13 → 31/12/17
Project: Fundamental
FWOAL586: Molecular mechanisms of intrinsically disordered proteins
Loris, R. & Haesaerts, S.
1/01/11 → 31/12/14
Project: Fundamental

1 Membership of external research organisation

Unknown (External organisation)
Alexandra Vandervelde (Member)
1 Oct 2008 → …
Activity: Membership › Membership of external research organisation

Cite this

@article{a9d2a3b202104bc19be79b5d7004e5b7,

title = "Crystallisation and preliminary X-ray analysis of two variants of the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex",

abstract = "The paaR2-paaA2-parE2 operon is a three-component toxin-antitoxin (TA) module encoded in the genome of the human pathogen E. coli O157. The toxin (ParE2) and antitoxin (PaaA2) interact to form a non-toxic antitoxin-toxin complex. In this paper, the crystallisation and preliminary characterisation of two variants of the PaaA2-ParE2 antitoxin-toxin complex are described. Seleno-methionine derivative crystals of the full-length PaaA2-ParE2 antitoxin-toxin complex diffract to 2.8 {\AA} and belong to space group P41212 (or P43212) with unit cell parameters a = b = 90.5 {\AA}, c = 412.3 {\AA}. In contrast, ParE2 and PaaA213-63, a truncated form of PaaA2 in which the first 12 N-terminal residues of the antitoxin have been deleted, form a hetero-dimer as evidenced by analytical gel filtration, dynamic light scattering, and small-angle X-ray scattering. Crystals of the PaaA213-63-ParE2 complex diffract to 2.7 {\AA} and belong to space group P6122 (or P6522) with unit cell parameters a = b = 91.6 {\AA}, c = 185.6 {\AA}.",

keywords = "structural biology, bacterial stress response, X-ray crystallography, toxin-antitoxin module, persistence",

author = "Yann Sterckx and Sarah Haesaerts and {Van Melderen}, Laurence and Remy Loris",

year = "2014",

language = "English",

volume = "70",

pages = "1284--1291",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Crystallisation and preliminary X-ray analysis of two variants of the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex

AU - Sterckx, Yann

AU - Haesaerts, Sarah

AU - Van Melderen, Laurence

AU - Loris, Remy

PY - 2014

Y1 - 2014

N2 - The paaR2-paaA2-parE2 operon is a three-component toxin-antitoxin (TA) module encoded in the genome of the human pathogen E. coli O157. The toxin (ParE2) and antitoxin (PaaA2) interact to form a non-toxic antitoxin-toxin complex. In this paper, the crystallisation and preliminary characterisation of two variants of the PaaA2-ParE2 antitoxin-toxin complex are described. Seleno-methionine derivative crystals of the full-length PaaA2-ParE2 antitoxin-toxin complex diffract to 2.8 Å and belong to space group P41212 (or P43212) with unit cell parameters a = b = 90.5 Å, c = 412.3 Å. In contrast, ParE2 and PaaA213-63, a truncated form of PaaA2 in which the first 12 N-terminal residues of the antitoxin have been deleted, form a hetero-dimer as evidenced by analytical gel filtration, dynamic light scattering, and small-angle X-ray scattering. Crystals of the PaaA213-63-ParE2 complex diffract to 2.7 Å and belong to space group P6122 (or P6522) with unit cell parameters a = b = 91.6 Å, c = 185.6 Å.

AB - The paaR2-paaA2-parE2 operon is a three-component toxin-antitoxin (TA) module encoded in the genome of the human pathogen E. coli O157. The toxin (ParE2) and antitoxin (PaaA2) interact to form a non-toxic antitoxin-toxin complex. In this paper, the crystallisation and preliminary characterisation of two variants of the PaaA2-ParE2 antitoxin-toxin complex are described. Seleno-methionine derivative crystals of the full-length PaaA2-ParE2 antitoxin-toxin complex diffract to 2.8 Å and belong to space group P41212 (or P43212) with unit cell parameters a = b = 90.5 Å, c = 412.3 Å. In contrast, ParE2 and PaaA213-63, a truncated form of PaaA2 in which the first 12 N-terminal residues of the antitoxin have been deleted, form a hetero-dimer as evidenced by analytical gel filtration, dynamic light scattering, and small-angle X-ray scattering. Crystals of the PaaA213-63-ParE2 complex diffract to 2.7 Å and belong to space group P6122 (or P6522) with unit cell parameters a = b = 91.6 Å, c = 185.6 Å.

KW - structural biology

KW - bacterial stress response

KW - X-ray crystallography

KW - toxin-antitoxin module

KW - persistence

M3 - Article

VL - 70

SP - 1284

EP - 1291

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

SN - 1744-3091

ER -

Crystallisation and preliminary X-ray analysis of two variants of the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex

Abstract

Keywords

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Projects

SRP13: Strategic Research Programme: Structure and dynamics of macromolecular complexes in health and disease

FWOAL699: ESRF and DUBBLE: Synchrotron X-rays for revealing the structure and function of molecules and materials

FWOAL586: Molecular mechanisms of intrinsically disordered proteins

Activities

Unknown (External organisation)

Cite this