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1mwm
From Proteopedia
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[[Image:1mwm.gif|left|200px]] | [[Image:1mwm.gif|left|200px]] | ||
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'''ParM from plasmid R1 ADP form''' | '''ParM from plasmid R1 ADP form''' | ||
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[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Moller-Jensen, J.]] | [[Category: Moller-Jensen, J.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:48:25 2008'' | |
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Revision as of 22:48, 2 May 2008
ParM from plasmid R1 ADP 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
1MWM 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 Sat May 3 01:48:25 2008
