ArticleActa crystallographica. Section D, Biological crystallography2015
Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Synergistic Antibacterial Efficacy of Melittin in Combination with Oxacillin against Methicillin-ResistantMicroorganisms · 2023Article
- Article
- The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Article
- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- An overview of moonlighting proteins in Staphylococcus aureus infection.Archives of microbiology · 2021Review
- Dramatic Changes in Oligomerization Property Caused by Single Residue Deletion in Staphylococcus aureus Enolase.Molecular biotechnology · 2021Article
- Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.Frontiers in molecular biosciences · 2021Article
- In silico prediction of a new lead compound targeting enolase of trypanosomatids through structure-based virtual screening and molecular dynamic studies.Journal of molecular modeling · 2020Article
- Immunization with recombinant enolase of Sporothrix spp. (rSsEno) confers effective protection against sporotrichosis in mice.Scientific reports · 2019Article
- Effect of ions and inhibitors on the catalytic activity and structural stability ofJournal of biosciences · 2019Article
- The Eno Gene of Burkholderia cenocepacia Strain 71-2 is Involved in Phosphate Solubilization.Current microbiology · 2019Article
- Featured Species-Specific Loops Are Found in the Crystal Structure ofFrontiers in cellular and infection microbiology · 2019Article
- Biochemical and Biophysical Characterization of the Enolase fromBioMed research international · 2018Article
- Crystal structure of enolase from Drosophila melanogaster.Acta crystallographica. Section F, Structural biology communications · 2017Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus is a Gram-positive bacterium with strong pathogenicity that causes a wide range of infections and diseases. Enolase is an evolutionarily conserved enzyme that plays a key role in energy production through glycolysis. Additionally, enolase is located on the surface of S. aureus and is involved in processes leading to infection. Here, crystal structures of Sa_enolase with and without bound phosphoenolpyruvate (PEP) are presented at 1.6 and 2.45 Å resolution, respectively. The structure reveals an octameric arrangement; however, both dimeric and octameric conformations were observed in solution. Furthermore, enzyme-activity assays show that only the octameric variant is catalytically active. Biochemical and structural studies indicate that the octameric form of Sa_enolase is enzymatically active in vitro and likely also in vivo, while the dimeric form is catalytically inactive and may be involved in other biological processes.
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