1mwm
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1mwm |SIZE=350|CAPTION= <scene name='initialview01'>1mwm</scene>, resolution 2.0Å | |PDB= 1mwm |SIZE=350|CAPTION= <scene name='initialview01'>1mwm</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mwk|1MWK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwm OCA], [http://www.ebi.ac.uk/pdbsum/1mwm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwm RCSB]</span> | ||
}} | }} | ||
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[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Moller-Jensen, J.]] | [[Category: Moller-Jensen, J.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: MG]] | ||
[[Category: parm]] | [[Category: parm]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:08 2008'' |
Revision as of 19:22, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1MWK
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:22:08 2008
