Open AccessOctameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate
Author(s) -
Wu Yunfei,
Wang Chengliang,
Lin Shenglong,
Wu Minhao,
Han Lu,
Tian Changlin,
Zhang Xuan,
Zang Jianye
Publication year - 2015
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004715018830
Subject(s) - enolase , staphylococcus aureus , phosphoenolpyruvate carboxykinase , lyase , enzyme , biochemistry , chemistry , biology , in vivo , bacteria , immunology , genetics , immunohistochemistry
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.