5BOF

Crystal Structure of Staphylococcus aureus Enolase

Summary for 5BOF

• Entry DOI: 10.2210/pdb5bof/pdb
• Related: 5BOE
• Descriptor: Enolase, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: enolase, lyase
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm : O69174
• Total number of polymer chains: 2
• Total formula weight: 97090.63

Authors

Wu, Y.F.,Wang, C.L.,Wu, M.H.,Han, L.,Zhang, X.,Zang, J.Y. (deposition date: 2015-05-27, release date: 2015-12-09, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.45 Å)