View source for 7bnr


==Crystal structure of a ParB Q52A mutant from Myxococcus xanthus bound to CTPyS==
<StructureSection load='7bnr' size='340' side='right'caption='[[7bnr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bnr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_DK_1622 Myxococcus xanthus DK 1622]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BNR 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UFQ:Cytosine+5-[gamma-thio]triphosphate'>UFQ</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=7bnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bnr OCA], [https://pdbe.org/7bnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bnr RCSB], [https://www.ebi.ac.uk/pdbsum/7bnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bnr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1CVJ4_MYXXD Q1CVJ4_MYXXD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ParB-like CTPases mediate the segregation of bacterial chromosomes and low-copy number plasmids. They act as DNA-sliding clamps that are loaded at parS motifs in the centromere of target DNA molecules and spread laterally to form large nucleoprotein complexes serving as docking points for the DNA segregation machinery. Here, we solve crystal structures of ParB in the pre- and post-hydrolysis state and illuminate the catalytic mechanism of nucleotide hydrolysis. Moreover, we identify conformational changes that underlie the CTP- and parS-dependent closure of ParB clamps. The study of CTPase-deficient ParB variants reveals that CTP hydrolysis serves to limit the sliding time of ParB clamps and thus drives the establishment of a well-defined ParB diffusion gradient across the centromere whose dynamics are critical for DNA segregation. These findings clarify the role of the ParB CTPase cycle in partition complex assembly and function and thus advance our understanding of this prototypic CTP-dependent molecular switch.

The CTPase activity of ParB determines the size and dynamics of prokaryotic DNA partition complexes.,Osorio-Valeriano M, Altegoer F, Das CK, Steinchen W, Panis G, Connolley L, Giacomelli G, Feddersen H, Corrales-Guerrero L, Giammarinaro PI, Hanssmann J, Bramkamp M, Viollier PH, Murray S, Schafer LV, Bange G, Thanbichler M Mol Cell. 2021 Sep 18. pii: S1097-2765(21)00738-3. doi:, 10.1016/j.molcel.2021.09.004. PMID:34562373<ref>PMID:34562373</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bnr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Myxococcus xanthus DK 1622]]
[[Category: Altegoer F]]
[[Category: Bange G]]