11xy: Difference between revisions

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'''Unreleased structure'''


The entry 11xy is ON HOLD  until Paper Publication
==Escherichia coli MurJ in the outward-facing conformation==
<StructureSection load='11xy' size='340' side='right'caption='[[11xy]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[11xy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=11XY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=11XY 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=11xy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11xy OCA], [https://pdbe.org/11xy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=11xy RCSB], [https://www.ebi.ac.uk/pdbsum/11xy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=11xy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MURJ_ECOLI MURJ_ECOLI] Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.[HAMAP-Rule:MF_02078]<ref>PMID:18708495</ref> <ref>PMID:18832143</ref> <ref>PMID:25013077</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan biogenesis requires membrane flippases to translocate lipid-linked precursors across the cytoplasmic membrane for processing. This essential step is mediated by MurJ, the lipid II flippase conserved across all peptidoglycan-producing bacteria. While MurJ from diderm bacteria has been structurally resolved in multiple conformational states, its monoderm homolog remains uncharacterized. Monoderm MurJ homologs exhibit substantial sequence divergence yet retain the same lipid II flipping function and are promising antibiotic targets. Here we report structures of Staphylococcus aureus MurJ (SaMurJ) captured in both outward- and inward-facing conformations. These structures show that SaMurJ adopts the conserved MOP family fold and undergoes conformational transitions consistent with an alternating-access mechanism. Our findings reveal conserved and divergent features of MurJ between diderm and monoderm bacteria that are critical for lipid II flipping and provide a structural framework for probing substrate recognition and specific inhibition.


Authors:  
Structures of the lipid II flippase from the monoderm pathogen Staphylococcus aureus.,Li YE, Baron GF, Clemons WM Jr J Biol Chem. 2026 Sep 5:113516. doi: 10.1016/j.jbc.2026.113516. PMID:42700959<ref>PMID:42700959</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 11xy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Clemons WM]]
[[Category: Li YE]]
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