Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila

Ekaterina V. Filippova, Chi Hao Luan, Sara F. Dunne, Olga Kiryukhina, George Minasov, Ludmilla Shuvalova, Wayne F. Anderson*

*Corresponding author for this work

Research output: Contribution to journalArticle

3 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)33-40
Number of pages8
JournalJournal of Structural and Functional Genomics
Volume15
Issue number1
DOIs
StatePublished - Mar 2014

Keywords

  • Caci-0382
  • NTF2-like superfamily
  • Structural genomics
  • Trimethylamine
  • X-ray crystal structure

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

Fingerprint Dive into the research topics of 'Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila'. Together they form a unique fingerprint.

  • Cite this