1MWK
ParM from plasmid R1 APO form
Summary for 1MWK
Entry DOI | 10.2210/pdb1mwk/pdb |
Related | 1MWM |
Descriptor | ParM (2 entities in total) |
Functional Keywords | plasmid, plasmid partition, structural protein |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 71608.75 |
Authors | Van den Ent, F.,Moller-Jensen, J.,Amos, L.A.,Gerdes, K.,Lowe, J. (deposition date: 2002-09-30, release date: 2003-01-28, Last modification date: 2024-03-13) |
Primary citation | Van den Ent, F.,Moller-Jensen, J.,Amos, L.A.,Gerdes, K.,Lowe, J. F-actin-like filaments formed by plasmid segregation protein ParM EMBO J., 21:6935-6943, 2002 Cited by PubMed Abstract: It was the general belief that DNA partitioning in prokaryotes is independent of a cytoskeletal structure, which in eukaryotic cells is indispensable for DNA segregation. Recently, however, immunofluorescence microscopy revealed highly dynamic, filamentous structures along the longitudinal axis of Escherichia coli formed by ParM, a plasmid-encoded protein required for accurate segregation of low-copy-number plasmid R1. We show here that ParM polymerizes into double helical protofilaments with a longitudinal repeat similar to filamentous actin (F-actin) and MreB filaments that maintain the cell shape of non-spherical bacteria. The crystal structure of ParM with and without ADP demonstrates that it is a member of the actin family of proteins and shows a domain movement of 25 degrees upon nucleotide binding. Furthermore, the crystal structure of ParM reveals major differences in the protofilament interface compared with F-actin, despite the similar arrangement of the subunits within the filaments. Thus, there is now evidence for cytoskeletal structures, formed by actin-like filaments that are involved in plasmid partitioning in E.coli. PubMed: 12486014DOI: 10.1093/emboj/cdf672 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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