Functional clues from the crystal structure of an orphan periplasmic ligand-binding protein fromTreponema pallidum
| Autor: | Ranjit K. Deka, Diana R. Tomchick, Michael V. Norgard, Wei Z. Liu, Chad A. Brautigam |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Treponema biology 030106 microbiology Membrane biology ATP-binding cassette transporter Periplasmic space Ligand Binding Protein urologic and male genital diseases medicine.disease biology.organism_classification Biochemistry In vitro 03 medical and health sciences 030104 developmental biology medicine Syphilis Molecular Biology Pinta |
| Zdroj: | Protein Science. 26:847-856 |
| ISSN: | 0961-8368 |
| DOI: | 10.1002/pro.3133 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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