ParM from R1 plasmid in complex with peptide from C-terminus of ParRParM from R1 plasmid in complex with peptide from C-terminus of ParR

Structural highlights

4a62 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PARM_ECOLX Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid.

Publication Abstract from PubMed

To ensure their stable inheritance by daughter cells during cell division, bacterial low copy-number plasmids make simple DNA segregating machines that use an elongating protein filament between sister plasmids. In the ParMRC system of Escherichia coli R1 plasmid, ParM, an actin-like protein, forms the spindle between ParRC complexes on sister plasmids. Using a combination of structural work and total internal reflection fluorescence microscopy, we show that ParRC bound and could accelerate growth at only one end of polar ParM filaments, mechanistically resembling eukaryotic formins. The architecture of ParM filaments enabled two ParRC-bound filaments to associate in an antiparallel orientation, forming a bipolar spindle. The spindle elongated as a bundle of at least two antiparallel filaments, thereby pushing two plasmid clusters toward the poles.

A Bipolar Spindle of Antiparallel ParM Filaments Drives Bacterial Plasmid Segregation.,Gayathri P, Fujii T, Moller-Jensen J, van den Ent F, Namba K, Lowe J Science. 2012 Oct 25. PMID:23112295[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Gayathri P, Fujii T, Moller-Jensen J, van den Ent F, Namba K, Lowe J. A Bipolar Spindle of Antiparallel ParM Filaments Drives Bacterial Plasmid Segregation. Science. 2012 Oct 25. PMID:23112295 doi:http://dx.doi.org/10.1126/science.1229091

4a62, resolution 2.20Å

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