4MKS

Crystal structure of enolase from Lactobacillus gasseri

Summary for 4MKS

• Entry DOI: 10.2210/pdb4mks/pdb
• Related: 1w6t 4a3r 4ewj
• Descriptor: Enolase 2, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: enolase, lyase
• Biological source: Lactobacillus gasseri
• Cellular location: Cytoplasm (By similarity): Q042F4
• Total number of polymer chains: 2
• Total formula weight: 96086.99

Authors

Raghunathan, K.,Harris, P.T.,Spurbeck, R.R.,Arvidson, C.G.,Arvidson, D.N. (deposition date: 2013-09-05, release date: 2014-05-21, Last modification date: 2023-09-20)

Primary citation

Raghunathan, K.,Harris, P.T.,Spurbeck, R.R.,Arvidson, C.G.,Arvidson, D.N.
Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri.
Febs Lett., 588:2212-2216, 2014

PubMed 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.

PubMed: 24859038
DOI: 10.1016/j.febslet.2014.05.020

Experimental method

X-RAY DIFFRACTION (2.079 Å)