View source for 9s99


==CdvB2 filament - high twist, class B==
<StructureSection load='9s99' size='340' side='right'caption='[[9s99]], [[Resolution|resolution]] 3.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9s99]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9S99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S99 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]] 3.98&#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=9s99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s99 OCA], [https://pdbe.org/9s99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s99 RCSB], [https://www.ebi.ac.uk/pdbsum/9s99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s99 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDVB2_SULAC CDVB2_SULAC] Part of a cell division machinery.<ref>PMID:24399085</ref> 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9s99" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus acidocaldarius]]
[[Category: Drobnic T]]
[[Category: Lowe J]]