Evidence map›Paper›PMID 33376139›Full record

ArticleThe Journal of biological chemistry

Structure and mechanism of Staphylococcus aureus oleate hydratase (OhyA).

Christopher D Radka, Justin L Batte, Matthew W Frank, Brandon M Young, Charles O Rock

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 10% of its field
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

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. A Comparative Biochemical Study of Oleate Hydratases.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Article
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  5. Review
  6. Review
  7. Article
  8. Article
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  10. Convergent reductive evolution in bee-associated lactic acid bacteria.bioRxiv : the preprint server for biology · 2024
    Article
  11. Review
  12. Frontiers in cellular and infection microbiology · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. VaginalbioRxiv : the preprint server for biology · 2023
    Article
  17. Chiral Alcohols from Alkenes and Water: Directed Evolution of a Styrene Hydratase.Angewandte Chemie (International ed. in English) · 2023
    Article
  18. Review
  19. Article
  20. Novel oleate hydratases and potential biotechnological applications.Applied microbiology and biotechnology · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Christopher D RadkaThe Department of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Justin L BatteThe Department of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Matthew W FrankThe Department of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Brandon M YoungDepartment of Chemical Biology and Therapeutics, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Charles O RockThe Department of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA. Electronic address: charles.rock@stjude.org.
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
REGULATION OF LIPID METABOLISM IN E COLIR01GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 1985 to 2022
$9.2M
REGULATION OF LIPID METABOLISM IN BACTERIAR37GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 2001 to 2010
$5.7M
Training in the Design and Development of Infectious Disease TherapeuticsT32AI106700 · NIAID · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI Richard E. Lee · 2015 to 2026
$2.1M
NCI NIH HHS P30 CA021765NIAID NIH HHS T32 AI106700NIGMS NIH HHS R01 GM034496NIGMS NIH HHS R37 GM034496
6 · The paper itself

Abstract

Flavin adenine dinucleotide (FAD)-dependent bacterial oleate hydratases (OhyAs) catalyze the addition of water to isolated fatty acid carbon-carbon double bonds. Staphylococcus aureus uses OhyA to counteract the host innate immune response by inactivating antimicrobial unsaturated fatty acids. Mechanistic information explaining how OhyAs catalyze regiospecific and stereospecific hydration is required to understand their biological functions and the potential for engineering new products. In this study, we deduced the catalytic mechanism of OhyA from multiple structures of S. aureus OhyA in binary and ternary complexes with combinations of ligands along with biochemical analyses of relevant mutants. The substrate-free state shows Arg81 is the gatekeeper that controls fatty acid entrance to the active site. FAD binding engages the catalytic loop to simultaneously rotate Glu82 into its active conformation and Arg81 out of the hydrophobic substrate tunnel, allowing the fatty acid to rotate into the active site. FAD binding also dehydrates the active site, leaving a single water molecule connected to Glu82. This active site water is a hydronium ion based on the analysis of its hydrogen bond network in the OhyA•PEG400•FAD complex. We conclude that OhyA accelerates acid-catalyzed alkene hydration by positioning the fatty acid double bond to attack the active site hydronium ion, followed by the addition of water to the transient carbocation intermediate. Structural transitions within S. aureus OhyA channel oleate to the active site, curl oleate around the substrate water, and stabilize the hydroxylated product to inactivate antimicrobial fatty acids.

Indexed as

Bacterial ProteinsCatalysisCatalytic DomainCrystallography, X-RayFatty Acids, UnsaturatedHumansHydro-LyasesOleic AcidProtein ConformationStaphylococcal InfectionsStaphylococcus aureusSubstrate SpecificityBacterial ProteinsFatty Acids, UnsaturatedHydro-LyasesOleic Acidbacteriaenzyme catalysisfatty acid metabolismflavin adenine dinucleotide (FAD)oleate hydratase (OhyA)Staphylococcus aureus (S. aureus)X-ray crystallography

Identifiers

PMID33376139
PMCPMC7948970
OpenAlexW3116072518

What OpenQuestion holds

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LicenceCC BY
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.