1mwk
From Proteopedia
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ParM from plasmid R1 APO form
Overview
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.
About this Structure
1MWK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
F-actin-like filaments formed by plasmid segregation protein ParM., van den Ent F, Moller-Jensen J, Amos LA, Gerdes K, Lowe J, EMBO J. 2002 Dec 16;21(24):6935-43. PMID:12486014
Page seeded by OCA on Tue Nov 20 21:46:00 2007
