View source for 2xj4


==Structure of the bacterial cell division regulator protein MipZ==
<StructureSection load='2xj4' size='340' side='right'caption='[[2xj4]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XJ4 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]] 1.6&#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=2xj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xj4 OCA], [https://pdbe.org/2xj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xj4 RCSB], [https://www.ebi.ac.uk/pdbsum/2xj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xj4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3CA70_CAUVN A0A0H3CA70_CAUVN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein gradients play a central role in the spatial organization of cells, but the mechanisms of their formation are incompletely understood. This study analyzes the determinants responsible for establishing bipolar gradients of the ATPase MipZ, a key regulator of division site placement in Caulobacter crescentus. We have solved the crystal structure of MipZ in different nucleotide states, dissected its ATPase cycle, and investigated its interaction with FtsZ, ParB, and the nucleoid. Our results suggest that the polar ParB complexes locally stimulate the formation of ATP-bound MipZ dimers, which are then retained near the cell poles through association with chromosomal DNA. Due to their intrinsic ATPase activity, dimers eventually dissociate into freely diffusible monomers that undergo spontaneous nucleotide exchange and are recaptured by ParB. These findings clarify the molecular function of a conserved gradient-forming system and reveal mechanistic principles that might be commonly used to sustain protein gradients within cells.

Localized Dimerization and Nucleoid Binding Drive Gradient Formation by the Bacterial Cell Division Inhibitor MipZ.,Kiekebusch D, Michie KA, Essen LO, Lowe J, Thanbichler M Mol Cell. 2012 May 11;46(3):245-59. Epub 2012 Apr 5. PMID:22483621<ref>PMID:22483621</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xj4" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Caulobacter vibrioides]]
[[Category: Large Structures]]
[[Category: Lowe J]]
[[Category: Michie KA]]