1mwk: Difference between revisions
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[[Image:1mwk.gif|left|200px]] | [[Image:1mwk.gif|left|200px]] | ||
'''ParM from plasmid R1 APO form''' | {{Structure | ||
|PDB= 1mwk |SIZE=350|CAPTION= <scene name='initialview01'>1mwk</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= parM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''ParM from plasmid R1 APO form''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MWK is a [ | 1MWK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWK OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12486014 12486014] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: plasmid partition]] | [[Category: plasmid partition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:11 2008'' | ||
Revision as of 10:49, 20 March 2008
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| 1mwk, resolution 2.3Å | |||||||||||||
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| Gene: | parM (Escherichia coli) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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