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

Abstract

a b s t r a c tEnolases 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 2.08 Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function. Structured summary of protein interactions:Eno and eno bind by X-ray crystallography (View interaction)

Molecular Docking of Bacterial Protein Modulators and Pharmacotherapeutics of Carica papaya Leaves as a Promising Therapy for Sepsis: Synchronising In Silico and In Vitro Studies

“…The 3D structure of heat shock protein (PDB ID: 4PO2), surfactant protein D (PDB ID: 1PW9), and lactobacillus bacterial protein (4MKS) was performed on a Maestro 12.5 program (Schrodinger Inc., New York, NY, USA) using a the 64-bit operating system [Intel (R) Core (TM) i3-7020U CPU @ 2.30 GHz, 8 GB RAM]. The X-ray crystal structure, heat shock protein (PDB ID: 4PO2) [ 37 ], surfactant protein D (PDB ID: 1PW9) [ 38 ], and lactobacillus bacterial protein (PDB ID: 4MKS) [ 39 ] with the known inhibitor (imipenem and cyclophosphamide), was retrieved from the RCSB protein Data Bank ( accessed on 26 July 2022). The protein obtained was first prepared using the protein preparation wizard module.…”

An integrated metagenome and -proteome analysis of the microbial community residing in a biogas production plant

“…Commonly, enolases are involved in carbon metabolism. For example, an enolase catalyzes the reversible reaction from 2phosphoglycerate to phosphoenolpyruvate (Raghunathan et al, 2014). In total, contig 58257000014 harbors 22 genes.…”

Characterization and Structural Analyses of Enolase from Shrimp (Litopenaeus vannamei)

“…The structures of enolases from various species such as Lactobacillus gasseri (4MKS), Escherichia coli (1E9I), Homo sapiens (3B97), and others have been elucidated. The first reported crystal structure is that of yeast enolase (3ENL). , The primary structural framework of enolase is highly conserved, featuring each subunit comprising a smaller N-terminal domain and a longer C-terminal domain.…”

“…The enzyme activity center site is located in the folded cavity of the C-terminal barrel domain. In most organisms, enolase exists as a dimer, composed of two monomers arranged in a reverse parallel manner, while in a few organisms, it also forms an octamer. ,, Moreover, within the realm of crustaceans and other species, enolase stands as a potential allergenic substance, alongside well-known allergens like tropomyosin, arginine kinase, and hemocyanin. − Previous research has already recognized enolase as one of the allergens in L. vannamei through transcriptome analysis .…”

“…17 by increased glucose metabolism, so enolase holds significant importance in both tumor diagnosis and prognosis. 18 The structures of enolases from various species such as Lactobacillus gasseri (4MKS), 19 Escherichia coli (1E9I), 20 Homo sapiens (3B97), 21 and others have been elucidated. The first reported crystal structure is that of yeast enolase (3ENL).…”