6ryk: Difference between revisions

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'''Unreleased structure'''


The entry 6ryk is ON HOLD  until Paper Publication
==Crystal structure of the ParB-like protein PadC==
<StructureSection load='6ryk' size='340' side='right'caption='[[6ryk]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ryk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RYK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ryk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ryk OCA], [http://pdbe.org/6ryk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ryk RCSB], [http://www.ebi.ac.uk/pdbsum/6ryk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ryk ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During cell division, newly replicated DNA is actively segregated to the daughter cells. In most bacteria, this process involves the DNA-binding protein ParB, which condenses the centromeric regions of sister DNA molecules into kinetochore-like structures that recruit the DNA partition ATPase ParA and the prokaroytic SMC/condensin complex. Here, we report the crystal structure of a ParB-like protein (PadC) that emerges to tightly bind the ribonucleotide CTP. The CTP-binding pocket of PadC is conserved in ParB and composed of signature motifs known to be essential for ParB function. We find that ParB indeed interacts with CTP and requires nucleotide binding for DNA condensation in vivo. We further show that CTP-binding modulates the affinity of ParB for centromeric parS sites, whereas parS recognition stimulates its CTPase activity. ParB proteins thus emerge as a new class of CTP-dependent molecular switches that act in concert with ATPases and GTPases to control fundamental cellular functions.


Authors: Altegoer, F., Bange, G.
ParB-type DNA Segregation Proteins Are CTP-Dependent Molecular Switches.,Osorio-Valeriano M, Altegoer F, Steinchen W, Urban S, Liu Y, Bange G, Thanbichler M Cell. 2019 Dec 12;179(7):1512-1524.e15. doi: 10.1016/j.cell.2019.11.015. PMID:31835030<ref>PMID:31835030</ref>


Description: Crystal structure of the ParB-like protein PadC
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6ryk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Altegoer, F]]
[[Category: Bange, G]]
[[Category: Bange, G]]
[[Category: Altegoer, F]]
[[Category: Bactofilin]]
[[Category: Cell cycle]]
[[Category: Ctp]]
[[Category: Cytoskeleton]]
[[Category: Parab]]
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