Crystallization of the C-terminal domain of the addiction antidote CcdA in complex with its toxin CcdB.

TitleCrystallization of the C-terminal domain of the addiction antidote CcdA in complex with its toxin CcdB.
Publication TypeJournal Article
Year of Publication2005
AuthorsButs, L., N. De Jonge, R. Loris, L. Wyns, and M-H. Dao-Thi
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume61
IssuePt 10
Pagination949-52
Date Published2005 Oct 1
ISSN1744-3091
KeywordsBacterial Proteins, Bacterial Toxins, Crystallization, Crystallography, X-Ray, Dimerization, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Evolution, Molecular, Membrane Proteins, Models, Statistical, Plasmids, Protein Conformation, Protein Structure, Tertiary, Toxins, Biological, X-Ray Diffraction
Abstract

CcdA and CcdB are the antidote and toxin of the ccd addiction module of Escherichia coli plasmid F. The CcdA C-terminal domain (CcdAC36; 36 amino acids) was crystallized in complex with CcdB (dimer of 2 x 101 amino acids) in three different crystal forms, two of which diffract to high resolution. Form II belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.6, b = 60.5, c = 83.8 A and diffracts to 1.8 A resolution. Form III belongs to space group P2(1), with unit-cell parameters a = 41.0, b = 37.9, c = 69.6 A, beta = 96.9 degrees, and diffracts to 1.9 A resolution.

DOI10.1107/S1744309105029258
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID16511204
PubMed Central IDPMC1991321