ArticleActa crystallographica. Section F, Structural biology communications2018
Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- The power of DNA-encoded chemical libraries in the battle against drug-resistant bacteria.RSC advances · 2025Review
- Genetic synergy betweenmBio · 2024Article
- Investigations into the Antibacterial Mechanism of Action of Viridicatumtoxins.ACS infectious diseases · 2020Article
- Cocktailed fragment screening by X-ray crystallography of the antibacterial target undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structural Characterization of Full-Length Human Dehydrodolichyl Diphosphate Synthase Using an Integrative Computational and Experimental Approach.Biomolecules · 2019Article
- Substrate-analogue complex structure of Mycobacterium tuberculosis decaprenyl diphosphate synthase.Acta crystallographica. Section F, Structural biology communications · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Undecaprenyl pyrophosphate (UPP) is an important carrier of the oligosaccharide component in peptidoglycan synthesis. Inhibition of UPP synthase (UPPS) may be an effective strategy in combating the pathogen Acinetobacter baumannii, which has evolved to be multidrug-resistant. Here, A. baumannii UPPS (AbUPPS) was cloned, expressed, purified and crystallized, and its structure was determined by X-ray diffraction. Each chain of the dimeric protein folds into a central β-sheet with several surrounding α-helices, including one at the C-terminus. In the active site, two molecules of citrate interact with the side chains of the catalytic aspartate and serine. These observations may provide a structural basis for inhibitor design against AbUPPS.
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Registered trials
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