Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ.

@article{Cordell2003CrystalSO,
  title={Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ.},
  author={Suzanne C. Cordell and Elva J. H. Robinson and James L. Lowe},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 13},
  pages={
          7889-94
        }
}
SulA halts cell division in Escherichia coli by binding to the major component of the division machinery FtsZ. We have solved the crystal structure of SulA alone and in complex with FtsZ from Pseudomonas aeruginosa. SulA is expressed when the SOS response is induced. This is a mechanism to inhibit cell division and repair DNA in the event of DNA damage. FtsZ is a tubulin-like protein that forms polymers, with the active-site GTPase split across two monomers. One monomer provides the GTP-binding… CONTINUE READING

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Recent Changes to the MOSFLM Package for Processing Film and Image Plate Data (Science and Engineering Research Council Laboratory, Daresbury, Warrington, U.K.)

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