1mwk
From Proteopedia
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| - | [[Image:1mwk.gif|left|200px]] | + | [[Image:1mwk.gif|left|200px]] |
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| - | '''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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| , 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
Page seeded by OCA on Thu Mar 20 12:49:11 2008
