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| [[Image:1mwk.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1mwk| PDB=1mwk | SCENE= }} | | {{STRUCTURE_1mwk| PDB=1mwk | SCENE= }} |
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| '''ParM from plasmid R1 APO form'''
| | ===ParM from plasmid R1 APO form=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12486014}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12486014 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12486014}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Plasmid]] | | [[Category: Plasmid]] |
| [[Category: Plasmid partition]] | | [[Category: Plasmid partition]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:48:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:12:00 2008'' |
