5BOF

Crystal Structure of Staphylococcus aureus Enolase

5BOF の概要

• エントリーDOI: 10.2210/pdb5bof/pdb
• 関連するPDBエントリー: 5BOE
• 分子名称: Enolase, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: enolase, lyase
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm : O69174
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97090.63

構造登録者

Wu, Y.F.,Wang, C.L.,Wu, M.H.,Han, L.,Zhang, X.,Zang, J.Y. (登録日: 2015-05-27, 公開日: 2015-12-09, 最終更新日: 2023-11-08)

主引用文献

Wu, Y.,Wang, C.,Lin, S.,Wu, M.,Han, L.,Tian, C.,Zhang, X.,Zang, J.
Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate.
Acta Crystallogr.,Sect.D, 71:2457-2470, 2015

PubMed 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.

PubMed: 26627653
DOI: 10.1107/S1399004715018830

実験手法

X-RAY DIFFRACTION (2.45 Å)