title: Structural characterization of a hypothetical protein: a potential agent involved in trimethylamine metabolism in Catenulispora acidiphila.
abstract: Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci_0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci_0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci_0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.
authors.affiliation: Department of Molecular Pharmacology and Biological Chemistry, Northwestern Feinberg School of Medicine, Chicago, IL, 60611, USA.
authors.forename: Ekaterina V
authors.initials: EV
authors.lastname: Filippova
authors.forename: Chi-Hao
authors.initials: CH
authors.lastname: Luan
authors.forename: Sara F
authors.initials: SF
authors.lastname: Dunne
authors.forename: Olga
authors.initials: O
authors.lastname: Kiryukhina
authors.forename: George
authors.initials: G
authors.lastname: Minasov
authors.forename: Ludmilla
authors.initials: L
authors.lastname: Shuvalova
authors.forename: Wayne F
authors.initials: WF
authors.lastname: Anderson
mesh_terms: D000192:Actinomycetales / Q000201:enzymology*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000648:ultrastructure*; D020134:Catalytic Domain; D003001:Cloning, Molecular; D004851:Epoxide Hydrolases / Q000235:genetics / Q000648:ultrastructure*; D008024:Ligands; D008744:Methylamines / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D008024:Ligands; D008744:Methylamines; D004851:Epoxide Hydrolases; C115926:limonene-1,2-epoxide hydrolase; C023336:trimethylamine