4A6J

Structural model of ParM filament based on CryoEM map

Summary for 4A6J

• Entry DOI: 10.2210/pdb4a6j/pdb
• Related: 1MWK 1MWM 4A61 4A62
• EMDB information: 1980
• Descriptor: PLASMID SEGREGATION PROTEIN PARM, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total)
• Functional Keywords: transport protein
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 10
• Total formula weight: 363348.76

Authors

Gayathri, P.,Fujii, T.,Moller-Jensen, J.,Van Den Ent, F.,Namba, K.,Lowe, J. (deposition date: 2011-11-04, release date: 2012-11-21, Last modification date: 2024-05-08)

Primary citation

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, 338:1334-, 2012

PubMed Abstract: 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 the Escherichia coli R1 plasmid, ParM, an actinlike protein, forms the spindle between ParRC complexes on sister plasmids. By 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.

PubMed: 23112295
DOI: 10.1126/SCIENCE.1229091

Experimental method

ELECTRON MICROSCOPY (7.2 Å)