View source for 8aks


==215 A SynPspA rod after incubation with ATP==
<StructureSection load='8aks' size='340' side='right'caption='[[8aks]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8aks]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AKS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#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=8aks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aks OCA], [https://pdbe.org/8aks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aks RCSB], [https://www.ebi.ac.uk/pdbsum/8aks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aks ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P74717_SYNY3 P74717_SYNY3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic members of the endosome sorting complex required for transport-III (ESCRT-III) family have been shown to form diverse higher-order assemblies. The bacterial phage shock protein A (PspA) has been identified as a member of the ESCRT-III superfamily, and PspA homo-oligomerizes to form rod-shaped assemblies. As observed for eukaryotic ESCRT-III, PspA forms tubular assemblies of varying diameters. Using electron cryo-electron microscopy, we determined 61 Synechocystis PspA structures and observed in molecular detail how the structural plasticity of PspA rods is mediated by conformational changes at three hinge regions in the monomer and by the fixed and changing molecular contacts between protomers. Moreover, we reduced and increased the structural plasticity of PspA rods by removing the loop connecting helices alpha3/alpha4 and the addition of nucleotides, respectively. Based on our analysis of PspA-mediated membrane remodeling, we suggest that the observed mode of structural plasticity is a prerequisite for the biological function of ESCRT-III members.

Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.,Junglas B, Hudina E, Schonnenbeck P, Ritter I, Heddier A, Santiago-Schubel B, Huesgen PF, Schneider D, Sachse C Nat Struct Mol Biol. 2024 Aug 16. doi: 10.1038/s41594-024-01359-7. PMID:39152237<ref>PMID:39152237</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8aks" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Hudina E]]
[[Category: Huesgen P]]
[[Category: Junglas B]]
[[Category: Ritter I]]
[[Category: Sachse C]]
[[Category: Santiago-Schuebel B]]
[[Category: Schoennenbeck P]]