ZnuABC

High-affinity zinc uptake system protein ZnuA

The structure of ZnuA bound to zinc (gray sphere), with coordinating amino acids shown in white. From PDB: 2OSV.[1]
Identifiers
Organism Escherichia coli
Symbol ZnuA
PDB 2OSV
UniProt P39172
High-affinity zinc uptake system membrane protein ZnuB
Identifiers
Organism Escherichia coli
Symbol ZnuB
UniProt P39832
High-affinity zinc uptake system membrane protein ZnuC
Identifiers
Organism Escherichia coli
Symbol ZnuC
UniProt P0A9X1

ZnuABC is a high-affinity transporter specialized for transporting zinc ions as part of a system for metal ion homeostasis in bacteria. The complex is a member of the ATP-binding cassette (ABC) transporter protein family. The transporter contains three protein components:[2][3]

The expression of ZnuABC is regulated by the zinc uptake regulator (Zur) protein and is induced by conditions of zinc starvation. Because zinc is often a limiting factor in bacterial infections, some pathogenic bacteria are heavily dependent on ZnuABC to scavenge zinc from the environment in an animal host.[4]

The periplasmic protein ZnuA interacts with ZinT, another component of the regulon controlled by Zur, which is also involved in periplasmic zinc homeostasis.[4][5][6][7]

References

  1. Li, H; Jogl, G (18 May 2007). "Crystal structure of the zinc-binding transport protein ZnuA from Escherichia coli reveals an unexpected variation in metal coordination.". Journal of Molecular Biology. 368 (5): 1358–66. doi:10.1016/j.jmb.2007.02.107. PMID 17399739.
  2. Patzer, SI; Hantke, K (June 1998). "The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli.". Molecular Microbiology. 28 (6): 1199–210. doi:10.1046/j.1365-2958.1998.00883.x. PMID 9680209.
  3. Yatsunyk, LA; Easton, JA; Kim, LR; Sugarbaker, SA; Bennett, B; Breece, RM; Vorontsov, II; Tierney, DL; Crowder, MW; Rosenzweig, AC (February 2008). "Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli.". Journal of Biological Inorganic Chemistry. 13 (2): 271–88. doi:10.1007/s00775-007-0320-0. PMC 2630496Freely accessible. PMID 18027003.
  4. 1 2 Gabbianelli, R; Scotti, R; Ammendola, S; Petrarca, P; Nicolini, L; Battistoni, A (21 February 2011). "Role of ZnuABC and ZinT in Escherichia coli O157:H7 zinc acquisition and interaction with epithelial cells.". BMC microbiology. 11: 36. doi:10.1186/1471-2180-11-36. PMC 3053223Freely accessible. PMID 21338480.
  5. Ilari, A; Alaleona, F; Tria, G; Petrarca, P; Battistoni, A; Zamparelli, C; Verzili, D; Falconi, M; Chiancone, E (January 2014). "The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.". Biochimica et Biophysica Acta. 1840 (1): 535–44. doi:10.1016/j.bbagen.2013.10.010. PMID 24128931.
  6. Petrarca, P; Ammendola, S; Pasquali, P; Battistoni, A (March 2010). "The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage.". Journal of Bacteriology. 192 (6): 1553–64. doi:10.1128/jb.01310-09. PMC 2832539Freely accessible. PMID 20097857.
  7. Blindauer, CA (18 March 2015). "Advances in the molecular understanding of biological zinc transport.". Chemical communications (Cambridge, England). 51 (22): 4544–63. doi:10.1039/c4cc10174j. PMID 25627157.


This article is issued from Wikipedia - version of the 7/30/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.