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


Publication Type:

Journal Article

Source:

Volume 61, Issue Pt 10, p.949 - 952 (2005)

URL:

PM:16511204

Keywords:

Bacterial Proteins; chemistry; Bacterial Toxins; Crystallization; Crystallography; X-Ray; Dimerization; Electrophoresis; Polyacrylamide Gel; Escherichia coli; metabolism; Evolution; Molecular; Membrane Proteins; Models; Statistical; Plasmids; Protein Conforma

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

Notes:

DA - 20060302
IS - 1744-3091 (Electronic)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Proteins)
RN - 0 (Bacterial Toxins)
RN - 0 (CcdA protein, Bacillus)
RN - 0 (CcdB protein, Plasmid F)
RN - 0 (Membrane Proteins)
RN - 0 (Toxins, Biological)
SB - IM