ArticleResearch square2026
X-ray Co-crystal Structure of a Novel Pseudomonas aeruginosa DXPS Inhibitor Reveals an Unusual Allosteric Binding Pocket.
Article in Research square, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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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.
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Authors and funding
12 authors.
Funding
Abstract
The enzyme 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) catalyzes the first and rate-limiting step of the methylerythritol 4-phosphate (MEP) pathway, representing a promising target for novel anti-infective agents. Given its essential role in the survival of Gram-negative pathogenic bacteria and its absence in humans, drug-discovery efforts to advance our understanding of this enzyme are urgently needed. Here, we unraveled a novel druggable allosteric pocket in DXPS, unexpectedly revealed through co-crystallization of tool compound
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Registered trials
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