View source for 7npd


==Vibiro cholerae ParA2==
<StructureSection load='7npd' size='340' side='right'caption='[[7npd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7npd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NPD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=7npd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7npd OCA], [https://pdbe.org/7npd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7npd RCSB], [https://www.ebi.ac.uk/pdbsum/7npd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7npd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9KKJ2_VIBCH Q9KKJ2_VIBCH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA's cooperative binding to DNA and the formation of high ParA density regions on the nucleoid.

The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding.,Parker AV, Mann D, Tzokov SB, Hwang LC, Bergeron JRC Nat Commun. 2021 Aug 27;12(1):5166. doi: 10.1038/s41467-021-25429-2. PMID:34453062<ref>PMID:34453062</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7npd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Bergeron JRC]]
[[Category: Parker AV]]