6DET

The crystal structure of Tv2483 bound to L-arginine

6DET の概要

• エントリーDOI: 10.2210/pdb6det/pdb
• 分子名称: Tv2483, ARGININE (3 entities in total)
• 機能のキーワード: abc transporter, amino-acid-binding protein, ligand-binding protein, transport protein
• 由来する生物種: Treponema vincentii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30372.44

構造登録者

Brautigam, C.A.,Norgard, M.V. (登録日: 2018-05-13, 公開日: 2019-03-20, 最終更新日: 2024-03-13)

主引用文献

Deka, R.K.,Liu, W.Z.,Tso, S.C.,Norgard, M.V.,Brautigam, C.A.
Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme.
Protein Sci., 27:2037-2050, 2018

PubMed Abstract: 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.

PubMed: 30242931
DOI: 10.1002/pro.3510

実験手法

X-RAY DIFFRACTION (1.75 Å)