Crystal structure of an efficacious gonococcal adherence inhibitor: an enolase from Lactobacillus gasseri

FEBS Lett. 2014 Jun 27;588(14):2212-6. doi: 10.1016/j.febslet.2014.05.020. Epub 2014 May 21.

Abstract

Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg(2+) cofactors. Determined using molecular replacement to 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.

Keywords: Enolase; Fibronectin; Lactobacillus gasseri; Moonlighting; Neisseria gonorrhoeae; Probiotics.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Lactobacillus / enzymology*
  • Magnesium / chemistry
  • Models, Molecular
  • Neisseria gonorrhoeae
  • Phosphopyruvate Hydratase / chemistry*
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Structural Homology, Protein

Substances

  • Bacterial Proteins
  • Phosphopyruvate Hydratase
  • Magnesium

Associated data

  • PDB/4MKS