5U2P

The crystal structure of Tp0737 from Treponema pallidum

5U2P の概要

• エントリーDOI: 10.2210/pdb5u2p/pdb
• 分子名称: Sugar ABC transporter substrate-binding protein, BROMIDE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: abc transporter, ligand-binding protein, transport protein
• 由来する生物種: Treponema pallidum subsp. pallidum (syphilis treponeme)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47931.07

構造登録者

Brautigam, C.A.,Deka, R.K.,Tomchick, D.R.,Norgard, M.V. (登録日: 2016-11-30, 公開日: 2017-02-22, 最終更新日: 2024-03-06)

主引用文献

Brautigam, C.A.,Deka, R.K.,Liu, W.Z.,Tomchick, D.R.,Norgard, M.V.
Functional clues from the crystal structure of an orphan periplasmic ligand-binding protein from Treponema pallidum.
Protein Sci., 26:847-856, 2017

PubMed Abstract: The spirochete Treponema pallidum is the causative agent of syphilis, a sexually transmitted infection of major global importance. Other closely related subspecies of Treponema also are the etiological agents of the endemic treponematoses, such as yaws, pinta, and bejel. The inability of T. pallidum and its close relatives to be cultured in vitro has prompted efforts to characterize T. pallidum's proteins structurally and biophysically, particularly those potentially relevant to treponemal membrane biology, with the goal of possibly revealing the functions of those proteins. This report describes the structure of the treponemal protein Tp0737; this polypeptide has a fold characteristic of a class of periplasmic ligand-binding proteins associated with ABC-type transporters. Although no ligand for the protein was observed in electron-density maps, and thus the nature of the native ligand remains obscure, the structural data described herein provide a foundation for further efforts to elucidate the ligand and thus the function of this protein in T. pallidum.

PubMed: 28168761
DOI: 10.1002/pro.3133

実験手法

X-RAY DIFFRACTION (1.76 Å)