Crystallization and preliminary X-ray diffraction analysis of the Bacillus subtilis replication termination protein in complex with the 37-base-pair TerI-binding site

The replication terminator protein (RTP) of Bacillus subtilis binds to specific DNA sequences that halt the progression of the replisome in a polar manner. These terminator complexes flank a defined region of the chromosome into which they allow replication forks to enter but not exit. Forcing the f...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-11, Vol.62 (11), p.1104-1107
Main Authors: Vivian, J. P., Porter, C., Wilce, J. A., Wilce, M. C. J.
Format: Article
Language:English
Subjects:
Bacillus subtilis
Bacillus subtilis - chemistry
Bacillus subtilis - genetics
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Base Pairing
Binding Sites
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization Communications
CRYSTALS
DNA
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - isolation & purification
Mutagenesis, Site-Directed
PROTEINS
Recombinant Proteins - chemistry
replication terminator proteins
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
TerI
Terminator Regions, Genetic
X-RAY DIFFRACTION
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Summary:The replication terminator protein (RTP) of Bacillus subtilis binds to specific DNA sequences that halt the progression of the replisome in a polar manner. These terminator complexes flank a defined region of the chromosome into which they allow replication forks to enter but not exit. Forcing the fusion of replication forks in a specific zone is thought to allow the coordination of post‐replicative processes. The functional terminator complex comprises two homodimers each of 29 kDa bound to overlapping binding sites. A preparation of RTP and a 37‐­base‐pair TerI sequence (comprising two binding sites for RTP) has been purified and crystallized. A data set to 3.9 Å resolution with 97.0% completeness and an Rsym of 12% was collected from a single flash‐cooled crystal using synchrotron radiation. The diffraction data are consistent with space group P622, with unit‐cell parameters a = b = 118.8, c = 142.6 Å.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309106039108