5aey: Difference between revisions

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'''Unreleased structure'''


The entry 5aey is ON HOLD
==actin-like ParM protein bound to AMPPNP==
<SX load='5aey' size='340' side='right' viewer='molstar' caption='[[5aey]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5aey]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AEY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5aey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aey OCA], [https://pdbe.org/5aey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aey RCSB], [https://www.ebi.ac.uk/pdbsum/5aey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aey ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PARM_ECOLX PARM_ECOLX] Involved in the control of plasmid partition. Required for the accurate segregation of the plasmid.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Active segregation of Escherichia coli low-copy-number plasmid R1 involves formation of a bipolar spindle made of left-handed double-helical actin-like ParM filaments. ParR links the filaments with centromeric parC plasmid DNA, while facilitating the addition of subunits to ParM filaments. Growing ParMRC spindles push sister plasmids to the cell poles. Here, using modern electron cryomicroscopy methods, we investigate the structures and arrangements of ParM filaments in vitro and in cells, revealing at near-atomic resolution how subunits and filaments come together to produce the simplest known mitotic machinery. To understand the mechanism of dynamic instability, we determine structures of ParM filaments in different nucleotide states. The structure of filaments bound to the ATP analogue AMPPNP is determined at 4.3 A resolution and refined. The ParM filament structure shows strong longitudinal interfaces and weaker lateral interactions. Also using electron cryomicroscopy, we reconstruct ParM doublets forming antiparallel spindles. Finally, with whole-cell electron cryotomography, we show that doublets are abundant in bacterial cells containing low-copy-number plasmids with the ParMRC locus, leading to an asynchronous model of R1 plasmid segregation.


Authors: Bharat, T.A.M., Murshudov, G.N., Sachse, C., Lowe, J.
Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles.,Bharat TA, Murshudov GN, Sachse C, Lowe J Nature. 2015 Apr 27:1-5. doi: 10.1038/nature14356. PMID:25915019<ref>PMID:25915019</ref>


Description: actin-like ParM protein bound to AMPPNP
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Murshudov, G.N]]
<div class="pdbe-citations 5aey" style="background-color:#fffaf0;"></div>
[[Category: Bharat, T.A.M]]
 
[[Category: Lowe, J]]
==See Also==
[[Category: Sachse, C]]
*[[Plasmid segregation protein ParM|Plasmid segregation protein ParM]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Bharat TAM]]
[[Category: Lowe J]]
[[Category: Murshudov GN]]
[[Category: Sachse C]]

Latest revision as of 14:40, 9 May 2024

actin-like ParM protein bound to AMPPNPactin-like ParM protein bound to AMPPNP

5aey, resolution 4.30Å

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