6xry: Difference between revisions

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'''Unreleased structure'''


The entry 6xry is ON HOLD
==Intrinsically disordered bacterial polar organizing protein Z, PopZ, interacts with protein binding partners through an N-terminal Molecular Recognition Feature==
<StructureSection load='6xry' size='340' side='right'caption='[[6xry]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XRY FirstGlance]. <br>
</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=6xry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xry OCA], [https://pdbe.org/6xry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xry RCSB], [https://www.ebi.ac.uk/pdbsum/6xry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xry ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9A8N4_CAUVC Q9A8N4_CAUVC]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The polar organizing protein Z (PopZ) is necessary for the formation of three-dimensional microdomains at the cell poles in Caulobacter crescentus, where it functions as a hub protein that recruits multiple regulatory proteins from the cytoplasm. Although a large portion of the protein is predicted to be natively unstructured, in reconstituted systems PopZ can self-assemble into a macromolecular scaffold that directly binds to at least ten different proteins. Here we report the solution NMR structure of PopZ(Delta134-177), a truncated form of PopZ that does not self-assemble but retains the ability to interact with heterologous proteins. We show that the unbound form of PopZ(Delta134-177) is unstructured in solution, with the exception of a small amphipathic alpha-helix in residues M10-I17, which is included within a highly conserved region near the N-terminus. In applying NMR techniques to map the interactions between PopZ(Delta134-177) and one of its binding partners, RcdA, we find evidence that the alpha-helix and adjoining amino acids extending to position E23 serve as the core of the binding motif. Consistent with this, a point mutation at position I17 severely compromises binding. Our results show that a partially structured Molecular Recognition Feature (MoRF) within an intrinsically disordered domain of PopZ contributes to the assembly of polar microdomains, revealing a structural basis for complex network assembly in Alphaproteobacteria that is analogous to those formed by intrinsically disordered hub proteins in other kingdoms.


Authors: Nordyke, C.T., Ahmed, Y., Puterbaugh, R.Z., Bowman, G.R., Varga, K.
Intrinsically disordered bacterial polar organizing protein Z, PopZ, interacts with protein binding partners through an N-terminal Molecular Recognition Feature.,Nordyke CT, Ahmed Y, Puterbaugh RZ, Bowman GR, Varga K J Mol Biol. 2020 Oct 12. pii: S0022-2836(20)30571-4. doi:, 10.1016/j.jmb.2020.09.020. PMID:33058876<ref>PMID:33058876</ref>


Description: Intrinsically disordered bacterial polar organizing protein Z, PopZ, interacts with protein binding partners through an N-terminal Molecular Recognition Feature
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Varga, K]]
<div class="pdbe-citations 6xry" style="background-color:#fffaf0;"></div>
[[Category: Bowman, G.R]]
== References ==
[[Category: Ahmed, Y]]
<references/>
[[Category: Nordyke, C.T]]
__TOC__
[[Category: Puterbaugh, R.Z]]
</StructureSection>
[[Category: Caulobacter vibrioides CB15]]
[[Category: Large Structures]]
[[Category: Ahmed YM]]
[[Category: Bowman GR]]
[[Category: Nordyke CT]]
[[Category: Puterbaugh RZ]]
[[Category: Varga K]]
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