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Crystallization of CcdB in complex with a GyrA fragment

Publication Type:

Journal Article

Authors:

Dao-Thi,M.H.; Van,Melderen L.; De,Genst E.; Buts,L.; Ranquin,A.; Wyns,L.; Loris,R.

Source:

Volume 60, Issue Pt 6, p.1132 - 1134 (2004)

URL:

PM:15159578

Keywords:

Bacterial Proteins; chemistry; Bacterial Toxins; Cloning; Molecular; Crystallography; X-Ray; DNA Gyrase; Dimerization; Electrophoresis; Polyacrylamide Gel; Escherichia coli; metabolism; F Factor; Plasmids; Protein Binding; Protein Structure; Tertiary; Surface

Abstract:

Plasmid addiction systems consist of a plasmid-encoded toxin-antidote pair that serves to stabilize low-copy-number plasmids in bacterial populations. CcdB, the toxin from the ccd system on the Escherichia coli F plasmid, acts as a gyrase poison. A 14 kDa fragment of gyrase, GyrA14, was found to bind to the toxin CcdB with an affinity of 1.75 x 10(-8) M. Crystals of the (GyrA14)(2) dimer in its free state belong to space group P4(3)2(1)2, with unit-cell parameters a = 86.4, c = 89.4 angstroms, and diffract to 2.4 angstroms. Crystals of the (GyrA14)(2)-(CcdB)(2) complex belong to space group P2(1)2(1)2(1), with a = 52.1, b = 83.3, c = 110.9 angstroms, and diffract to 2.8 angstroms resolution

Notes:

DA - 20040525
IS - 0907-4449 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Proteins)
RN - 0 (Bacterial Toxins)
RN - 0 (CcdB protein, Plasmid F)
RN - EC 5.99.1.- (DNA Gyrase)
SB - IM