Structures of the lipid II flippase from the monoderm pathogen Staphylococcus aureus.

Yancheng E Li, Grace F Baron, William M Clemons

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Yancheng E LiDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, USA.

Grace F BaronDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, USA.

William M ClemonsDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, USA; Chan Zuckerberg Initiative, Redwood City, California, USA. Electronic address: clemons@caltech.edu.

Funding

Mechanistic details of key integral-membrane enzymes for antimicrobial discoveryR01GM114611 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI William M. Clemons, Michio Kurosu · 2016 to 2026

$4.2M

NIGMS NIH HHS R01 GM114611

6 · The paper itself

Abstract

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.

Indexed as

antibioticsantibiotic targetcell walllipid flippaselipid IIlipid transportpeptidoglycan

Identifiers

PMID42700959

DOI10.1016/j.jbc.2026.113516

PMCPMC13661225

What OpenQuestion holds

Textmetadata

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.