Crystallization of Doc and the Phd:Doc toxin-antitoxin complex

Abel Garcia Pino; Hoa Dao-Thi Minh; Ehud Gazit; Roy Magnuson; Lode Wyns; Remy Loris

Crystallization of Doc and the Phd:Doc toxin-antitoxin complex

Abel Garcia Pino
, Hoa Dao-Thi Minh
, Ehud Gazit
, Roy Magnuson
, Lode Wyns
, Remy Loris

Department of Bio-engineering Sciences

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

The phd/doc addiction system is responsible for the stable inheritance of lysogenic bacteriophage P1 in its plasmidic form in Escherichia coli and is the archetype of a family of bacterial toxin-antitoxin modules. The His66Tyr mutant of Doc (DocH66Y) was crystallized in space group P21, with unit-cell parameters a = 53.1 A, b = 198.0 A, c = 54.1 A, beta = 93.0°. These crystals diffract to 2.5 A resolution and probably contain four dimers of Doc in the asymmetric unit. DocH66Y in complex with a 22-amino-acid C-terminal peptide of Phd (Phd52-73Se) was crystallized in space group C2, with unit-cell parameters a = 111.1 A, b = 38.6 A, c = 63.3 A, beta = 99.3°, and diffracted to 1.9 A resolution. Crystals of the complete wild-type Phd-Doc complex belong to space group P3121 or P3221, have an elongated unit cell with dimensions a = b = 48.9 A, c = 354.9 A and diffract to 2.4 A resolution using synchrotron radiation.

Original language	English
Pages (from-to)	1034-1038
Number of pages	5
Journal	Acta Crystallogr F Struct Biol Commun
Volume	64
Publication status	Published - 2008

Keywords

plasmid addiction
toxin-antitoxin
structural biology
ribosome inhibitor

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Persistent link

OZR1823: Structural basis of plasmid addiction and programmed cell death in bacteria
Loris, R. (Administrative Promotor)
1/10/08 → 30/09/09
Project: Fundamental
FWOAL381: Structural basis of plasmide addiction and programed cell death in bacteria
Haesaerts, S. (Mandate), De Greve, H. (Co-Promotor) & Loris, R. (Administrative Promotor)
1/01/06 → 31/12/09
Project: Fundamental
OZR1097: Crystallization of proteins
Loris, R. (Administrative Promotor)
1/01/05 → 31/12/05
Project: Fundamental

4 Talk or presentation at a workshop/seminar
3 Talk or presentation at a conference
2 Participation in conference
1 Membership of external research organisation

ESF-EMBO Symposium on Molecular Perspectives On Protein-Protein Interactions
De Gieter, S. (Speaker)
20 May 2013 → 25 May 2013
Activity: Talk or presentation › Talk or presentation at a conference
ESF-EMBO Symposium on Molecular Perspectives On Protein-Protein Interactions
Garcia Pino, A. (Participant)
20 May 2013 → 25 May 2013
Activity: Participating in or organising an event › Participation in conference
VIB Group Leader meeting
Loris, R. (Keynote speaker)
27 Jan 2012
Activity: Talk or presentation › Talk or presentation at a workshop/seminar

Cite this

@article{3828699f6205452db1da87f58f078c5c,

title = "Crystallization of Doc and the Phd:Doc toxin-antitoxin complex",

abstract = "The phd/doc addiction system is responsible for the stable inheritance of lysogenic bacteriophage P1 in its plasmidic form in Escherichia coli and is the archetype of a family of bacterial toxin-antitoxin modules. The His66Tyr mutant of Doc (DocH66Y) was crystallized in space group P21, with unit-cell parameters a = 53.1 A, b = 198.0 A, c = 54.1 A, beta = 93.0°. These crystals diffract to 2.5 A resolution and probably contain four dimers of Doc in the asymmetric unit. DocH66Y in complex with a 22-amino-acid C-terminal peptide of Phd (Phd52-73Se) was crystallized in space group C2, with unit-cell parameters a = 111.1 A, b = 38.6 A, c = 63.3 A, beta = 99.3°, and diffracted to 1.9 A resolution. Crystals of the complete wild-type Phd-Doc complex belong to space group P3121 or P3221, have an elongated unit cell with dimensions a = b = 48.9 A, c = 354.9 A and diffract to 2.4 A resolution using synchrotron radiation.",

keywords = "plasmid addiction, toxin-antitoxin, structural biology, ribosome inhibitor",

author = "\{Garcia Pino\}, Abel and \{Dao-Thi Minh\}, Hoa and Ehud Gazit and Roy Magnuson and Lode Wyns and Remy Loris",

year = "2008",

language = "English",

volume = "64",

pages = "1034--1038",

journal = "Acta Crystallogr F Struct Biol Commun",

issn = "1744-3091",

publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Crystallization of Doc and the Phd:Doc toxin-antitoxin complex

AU - Garcia Pino, Abel

AU - Dao-Thi Minh, Hoa

AU - Gazit, Ehud

AU - Magnuson, Roy

AU - Wyns, Lode

AU - Loris, Remy

PY - 2008

Y1 - 2008

N2 - The phd/doc addiction system is responsible for the stable inheritance of lysogenic bacteriophage P1 in its plasmidic form in Escherichia coli and is the archetype of a family of bacterial toxin-antitoxin modules. The His66Tyr mutant of Doc (DocH66Y) was crystallized in space group P21, with unit-cell parameters a = 53.1 A, b = 198.0 A, c = 54.1 A, beta = 93.0°. These crystals diffract to 2.5 A resolution and probably contain four dimers of Doc in the asymmetric unit. DocH66Y in complex with a 22-amino-acid C-terminal peptide of Phd (Phd52-73Se) was crystallized in space group C2, with unit-cell parameters a = 111.1 A, b = 38.6 A, c = 63.3 A, beta = 99.3°, and diffracted to 1.9 A resolution. Crystals of the complete wild-type Phd-Doc complex belong to space group P3121 or P3221, have an elongated unit cell with dimensions a = b = 48.9 A, c = 354.9 A and diffract to 2.4 A resolution using synchrotron radiation.

AB - The phd/doc addiction system is responsible for the stable inheritance of lysogenic bacteriophage P1 in its plasmidic form in Escherichia coli and is the archetype of a family of bacterial toxin-antitoxin modules. The His66Tyr mutant of Doc (DocH66Y) was crystallized in space group P21, with unit-cell parameters a = 53.1 A, b = 198.0 A, c = 54.1 A, beta = 93.0°. These crystals diffract to 2.5 A resolution and probably contain four dimers of Doc in the asymmetric unit. DocH66Y in complex with a 22-amino-acid C-terminal peptide of Phd (Phd52-73Se) was crystallized in space group C2, with unit-cell parameters a = 111.1 A, b = 38.6 A, c = 63.3 A, beta = 99.3°, and diffracted to 1.9 A resolution. Crystals of the complete wild-type Phd-Doc complex belong to space group P3121 or P3221, have an elongated unit cell with dimensions a = b = 48.9 A, c = 354.9 A and diffract to 2.4 A resolution using synchrotron radiation.

KW - plasmid addiction

KW - toxin-antitoxin

KW - structural biology

KW - ribosome inhibitor

M3 - Article

SN - 1744-3091

VL - 64

SP - 1034

EP - 1038

JO - Acta Crystallogr F Struct Biol Commun

JF - Acta Crystallogr F Struct Biol Commun

ER -

Crystallization of Doc and the Phd:Doc toxin-antitoxin complex

Abstract

Keywords

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Projects

OZR1823: Structural basis of plasmid addiction and programmed cell death in bacteria

FWOAL381: Structural basis of plasmide addiction and programed cell death in bacteria

OZR1097: Crystallization of proteins

Activities

ESF-EMBO Symposium on Molecular Perspectives On Protein-Protein Interactions

ESF-EMBO Symposium on Molecular Perspectives On Protein-Protein Interactions

VIB Group Leader meeting

Cite this