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1MWK

ParM from plasmid R1 APO form

Summary for 1MWK
Entry DOI10.2210/pdb1mwk/pdb
Related1MWM
DescriptorParM (2 entities in total)
Functional Keywordsplasmid, plasmid partition, structural protein
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight71608.75
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 citationVan 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: 12486014
DOI: 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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数据于2025-07-02公开中

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