4mks

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Crystal structure of enolase from Lactobacillus gasseriCrystal structure of enolase from Lactobacillus gasseri

Structural highlights

4mks is a 2 chain structure with sequence from Lactobacillus gasseri ATCC 33323 = JCM 1131. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.079Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

4mks, resolution 2.08Å

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OCA