Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate
Non-ligand-bound and PEP-bound structures of S. aureus enolase (Sa_enolase) were solved, and catalytic loop 1 in the PEP-bound structure was found to show both ‘open’ and ‘closed’ conformations. Structural and biochemical results indicate that octamerization is required for substrate binding and catalysis by Sa_enolase.