Structural highlights
Function
ENO2_LACGA Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).
Publication Abstract from PubMed
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 Mg2+ cofactors. Determined using molecular replacement to 2.08A, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.
Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri.,Raghunathan K, Harris PT, Spurbeck RR, Arvidson CG, Arvidson DN FEBS Lett. 2014 May 21. pii: S0014-5793(14)00392-5. doi:, 10.1016/j.febslet.2014.05.020. PMID:24859038[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Raghunathan K, Harris PT, Spurbeck RR, Arvidson CG, Arvidson DN. Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri. FEBS Lett. 2014 May 21. pii: S0014-5793(14)00392-5. doi:, 10.1016/j.febslet.2014.05.020. PMID:24859038 doi:http://dx.doi.org/10.1016/j.febslet.2014.05.020
