Journal Article

PHPPUBDB-8504

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Crystallization of Doc and the Phd-Doc toxin-antitoxin complex

Garcia-Pino, A. ; Dao-Thi, M. H. ; Gazit, E. ; Magnuson, R. D. ; Wyns, L. ; Loris, R. ; DESY

2008
Blackwell Oxford [u.a.]

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Please use a persistent id in citations: doi:10.1107/S1744309108031722

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 (Doc(H66Y)) was crystallized in space group P2(1), with unit-cell parameters a = 53.1, b = 198.0, c = 54.1 A, beta = 93.0 degrees . These crystals diffracted to 2.5 A resolution and probably contained four dimers of Doc in the asymmetric unit. Doc(H66Y) in complex with a 22-amino-acid C-terminal peptide of Phd (Phd(52-73Se)) was crystallized in space group C2, with unit-cell parameters a = 111.1, b = 38.6, c = 63.3 A, beta = 99.3 degrees , and diffracted to 1.9 A resolution. Crystals of the complete wild-type Phd-Doc complex belonged to space group P3(1)21 or P3(2)21, had an elongated unit cell with dimensions a = b = 48.9, c = 354.9 A and diffracted to 2.4 A resolution using synchrotron radiation.

Keyword(s): Antitoxins: chemistry (MeSH) ; Crystallization (MeSH) ; Molecular Sequence Data (MeSH) ; Multiprotein Complexes: chemistry (MeSH) ; Toxins, Biological: chemistry (MeSH) ; Viral Proteins: chemistry (MeSH) ; X-Ray Diffraction (MeSH) ; Antitoxins ; Doc protein, Enterobacteria phage P1 ; Multiprotein Complexes ; Phd protein, Enterobacteria phage P1 ; Toxins, Biological ; Viral Proteins

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Contributing Institute(s):

1. European Molecular Biology Laboratory (EMBL)

Research Program(s):

1. FS Beamline without reference (POF1-550) (POF1-550)

Experiment(s):

1. Unknown DESY Beamline

Appears in the scientific report 2008
Notes: (c) International Union of Crystallography.

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Database coverage:
; ; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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