9s9k: Difference between revisions
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==S. islandicus CdvB (semi open)== | |||
<StructureSection load='9s9k' size='340' side='right'caption='[[9s9k]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9s9k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus Sulfolobus islandicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9S9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S9K 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=9s9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s9k OCA], [https://pdbe.org/9s9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s9k RCSB], [https://www.ebi.ac.uk/pdbsum/9s9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s9k ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F0NEW1_SACI5 F0NEW1_SACI5] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Most prokaryotes divide using filaments of the tubulin-like FtsZ protein, while some archaea employ instead ESCRT-III-like proteins and their filaments for cell division and cytokinesis. The alternative archaeal system comprises Cdv proteins and is thought to bear some resemblance to ESCRT-III-based membrane remodeling in other domains of life, including eukaryotes, especially during abscission. Here, we present biochemical, crystallographic, and cryo-EM studies of the Sulfolobus Cdv machinery. CdvA, an early non-ESCRT component, adopts a PRC-domain/coiled-coil fold and polymerizes into long double-stranded helical filaments, mainly via hydrophobic interfaces. Monomeric CdvB adopts the canonical ESCRT-III fold in both a closed and a distinct "semiopen" conformation. Soluble CdvB2 filaments are composed of subunits in the closed state, appearing to transition to the open, active state only when polymerized on membranes. Short N-terminal amphipathic helices in all CdvB paralogues, B, B1, and B2, mediate membrane binding and are required for liposome recruitment in vitro. We provide a molecular overview of archaeal ESCRT-III-based cytokinesis machinery, the definitive demonstration that CdvB proteins are bona fide ESCRT-III homologues, and reveal the molecular basis for membrane engagement. Thus, we illuminate conserved principles of ESCRT-mediated membrane remodeling and extend them to an anciently diverged archaeal lineage. | |||
Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.,Drobnic T, Salzer R, Nierhaus T, Jiang MKX, Bellini D, Steindorf A, Albers SV, Baum B, Lowe J Proc Natl Acad Sci U S A. 2026 Jan 20;123(3):e2525941123. doi: , 10.1073/pnas.2525941123. Epub 2026 Jan 16. PMID:41543908<ref>PMID:41543908</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9s9k" style="background-color:#fffaf0;"></div> | ||
[[Category: Lowe | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfolobus islandicus]] | |||
[[Category: Lowe J]] | |||
[[Category: Salzer R]] | |||
