ArticleProtein science : a publication of the Protein Society2017
Functional clues from the crystal structure of an orphan periplasmic ligand-binding protein from Treponema pallidum.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Possible effects of Treponema pallidum infection on human vascular endothelial cells.Journal of clinical laboratory analysis · 2022Review
- Novel functional insights into a modified sugar-binding protein from Synechococcus MITS9220.Scientific reports · 2022Article
- Article
- Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme.Protein science : a publication of the Protein Society · 2018Article
- Functional insights from proteome-wide structural modeling of Treponema pallidum subspecies pallidum, the causative agent of syphilis.BMC structural biology · 2018Article
- The crystal structure of the Yersinia pestis iron chaperone YiuA reveals a basic triad binding motif for the chelated metal.Acta crystallographica. Section D, Structural biology · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
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