1mwk

<table><tr><td colspan='2'>[[1mwk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MWK FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mwm|1mwm]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">parM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwk OCA], [http://pdbe.org/1mwk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwk RCSB], [http://www.ebi.ac.uk/pdbsum/1mwk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwk ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PARM_ECOLX PARM_ECOLX]] Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12486014</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mwk" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Amos, L A]]

[[Category: Ent, F Van den]]

[[Category: Gerdes, K]]

[[Category: Lowe, J]]

[[Category: Moller-Jensen, J]]

[[Category: Plasmid]]

[[Category: Structural protein]]