Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme

Ranjit K. Deka, Wei Z. Liu, Shih Chia Tso, Michael V Norgard, Chad A Brautigam

Research output: Contribution to journalArticlepeer-review


Biophysical and biochemical studies on the lipoproteins and other periplasmic proteins from the spirochetal species Treponema pallidum have yielded numerous insights into the functioning of the organism's peculiar membrane organization, its nutritional requirements, and intermediary metabolism. However, not all T. pallidum proteins have proven to be amenable to biophysical studies. One such recalcitrant protein is Tp0309, a putative polar-amino-acid-binding protein of an ABC transporter system. To gain further information on its possible function, a homolog of the protein from the related species T. vincentii was used as a surrogate. This protein, Tv2483, was crystallized, resulting in the determination of its crystal structure at a resolution of 1.75 Å. The protein has a typical fold for a ligand-binding protein, and a single molecule of l-arginine was bound between its two lobes. Differential scanning fluorimetry and isothermal titration calorimetry experiments confirmed that l-arginine bound to the protein with unusually high selectivity. However, further comparison to Tp0309 showed differences in key amino-acid-binding residues may impart an alternate specificity for the T. pallidum protein.

Original languageEnglish (US)
Pages (from-to)2037-2050
Number of pages14
JournalProtein Science
Issue number12
StatePublished - Dec 2018


  • ABC transporter
  • Treponema
  • X-ray crystallography
  • differential scanning fluorimetry
  • isothermal titration calorimetry
  • l-arginine
  • ligand-binding protein
  • polar amino acids

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme'. Together they form a unique fingerprint.

Cite this