4A62
ParM from R1 plasmid in complex with peptide from C-terminus of ParR
Summary for 4A62
Entry DOI | 10.2210/pdb4a62/pdb |
Related | 1MWK 1MWM 4A61 |
Descriptor | PLASMID SEGREGATION PROTEIN PARM, PROTEIN STBB, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
Functional Keywords | transport protein, plasmid segregation |
Biological source | ESCHERICHIA COLI More |
Total number of polymer chains | 4 |
Total formula weight | 76606.13 |
Authors | Gayathri, P.,Lowe, J. (deposition date: 2011-10-31, release date: 2012-11-07, Last modification date: 2023-12-20) |
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 Cited by 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: 23112295DOI: 10.1126/SCIENCE.1229091 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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