9skl: Difference between revisions

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'''Unreleased structure'''


The entry 9skl is ON HOLD  until Paper Publication
==Polysaccharide co-polymerase FepE closed 9 subunit complex C9 symmetry==
<StructureSection load='9skl' size='340' side='right'caption='[[9skl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9skl]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9SKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SKL 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]] 2.8&#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=9skl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9skl OCA], [https://pdbe.org/9skl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9skl RCSB], [https://www.ebi.ac.uk/pdbsum/9skl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9skl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FEPE_ECOLI FEPE_ECOLI] Part of the ferric enterobactin transport system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lipopolysaccharides are important components of the gram-negative bacterial cell envelope that are involved in immune evasion and act as a protective barrier. Employing cryo-electron microscopy, we resolved the structure and dynamics of FepE, the copolymerase component of the Wzy-dependent pathway, responsible for the length modulation of very long O-antigen molecules. Comparison of the interior volumes of related copolymerases' periplasmic domains with the volume of hydrated sugars suggests that the size of the periplasmic domain controls the length of the O-antigen, implying that polysaccharide chain polymerization occurs inside the copolymerase periplasmic domain. Moreover, we show the opening of the FepE complex as well as other large mechanistically relevant movements. The opening of the complex presents an attractive corridor for the release of completed polysaccharide chains.


Authors: Wiseman, B., Hogbom, M.
Structural Basis of Lipopolysaccharide O-Antigen Chain Length Modality.,Wiseman B, Widmalm G, Hogbom M Research (Wash D C). 2026 May 12;9:1276. doi: 10.34133/research.1276. eCollection , 2026. PMID:42131584<ref>PMID:42131584</ref>


Description: Polysaccharide co-polymerase FepE closed 9 subunit complex C9 symmetry
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hogbom, M]]
<div class="pdbe-citations 9skl" style="background-color:#fffaf0;"></div>
[[Category: Wiseman, B]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Hogbom M]]
[[Category: Wiseman B]]

Latest revision as of 05:01, 27 May 2026

Polysaccharide co-polymerase FepE closed 9 subunit complex C9 symmetry

9skl, resolution 2.80Å

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