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

•First structure of enolase from Lactobacillus family, assembles as octamer.•First catalytic loop fully resolved in closed position.•Third catalytic loop disorder suggests high level of flexibility.•Described enolase may conserve putative plasminogen binding motif on catalytic loop. 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 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function. Eno and enobind by X-ray crystallography (View interaction)