ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families Pfam:PF01297,Pfam:PF00950, Pfam:PF00005, regulated by the transcription-regulator FUR, Pfam:PF01475 [2,3]. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), Pfam:PF01297 [4]. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination [1]. [1]. 12909634. YodA from Escherichia coli is a metal-binding, lipocalin-like. protein.. David G, Blondeau K, Schiltz M, Penel S, Lewit-Bentley A;. J Biol Chem. 2003;278:43728-43735.. [2]. 17931600. Zinc dependence of zinT (yodA) mutants and binding of zinc,. cadmium and mercury by ZinT.. Kershaw CJ, Brown NL, Hobman JL;. Biochem Biophys Res Commun. 2007;364:66-71.. [3]. 21338480. Role of ZnuABC and ZinT in Escherichia coli O157:H7 zinc. acquisition and interaction with epithelial cells.. Gabbianelli R, Scotti R, Ammendola S, Petrarca P, Nicolini L,. Battistoni A;. BMC Microbiol. 2011;11:36.. [4]. 24128931. The Salmonella enterica ZinT structure, zinc affinity and. interaction with the high-affinity uptake protein ZnuA provide. insight into the management of periplasmic zinc.. Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A,. Zamparelli C, Verzili D, Falconi M, Chiancone E;. Biochim Biophys Acta. 2014;1840:535-544. (from Pfam)
GO Terms:- Date:
- 2024-04-03