5BOE

Crystal structure of Staphylococcus aureus enolase in complex with PEP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.164 
  • R-Value Work: 0.148 
  • R-Value Observed: 0.149 

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This is version 1.2 of the entry. See complete history


Literature

Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate

Wu, Y.Wang, C.Lin, S.Wu, M.Han, L.Tian, C.Zhang, X.Zang, J.

(2015) Acta Crystallogr D Biol Crystallogr 71: 2457-2470

  • DOI: https://doi.org/10.1107/S1399004715018830
  • Primary Citation of Related Structures:  
    5BOE, 5BOF

  • 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.


  • Organizational Affiliation

    Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, Collaborative Innovation Center of Chemistry for Life Science, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Enolase
A, B
442Staphylococcus aureusMutation(s): 1 
Gene Names: eno
EC: 4.2.1.11
UniProt
Find proteins for O69174 (Staphylococcus aureus)
Explore O69174 
Go to UniProtKB:  O69174
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO69174
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.164 
  • R-Value Work: 0.148 
  • R-Value Observed: 0.149 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 145.154α = 90
b = 145.154β = 90
c = 100.512γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-12-09
    Type: Initial release
  • Version 1.1: 2015-12-16
    Changes: Database references
  • Version 1.2: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description