ZnuABC explained
| High-affinity zinc uptake system protein ZnuA |
| Organism: | Escherichia coli |
| Taxid: | 83333 |
| Symbol: | ZnuA |
| Pdb: | 2OSV |
| Uniprot: | P39172 |
| High-affinity zinc uptake system membrane protein ZnuB |
| Organism: | Escherichia coli |
| Taxid: | 83333 |
| Symbol: | ZnuB |
| Uniprot: | P39832 |
| High-affinity zinc uptake system membrane protein ZnuC |
| Organism: | Escherichia coli |
| Taxid: | 83333 |
| 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:[1] [2]
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.[3]
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]
Notes and References
- Patzer SI, Hantke K . The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli . Molecular Microbiology . 28 . 6 . 1199–210 . June 1998 . 9680209 . 10.1046/j.1365-2958.1998.00883.x . free .
- Yatsunyk LA, Easton JA, Kim LR, Sugarbaker SA, Bennett B, Breece RM, Vorontsov II, Tierney DL, Crowder MW, Rosenzweig AC . Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli . Journal of Biological Inorganic Chemistry . 13 . 2 . 271–88 . February 2008 . 18027003 . 2630496 . 10.1007/s00775-007-0320-0 .
- Gabbianelli R, Scotti R, Ammendola S, Petrarca P, Nicolini L, Battistoni A . Role of ZnuABC and ZinT in Escherichia coli O157:H7 zinc acquisition and interaction with epithelial cells . BMC Microbiology . 11 . 36 . February 2011 . 21338480 . 3053223 . 10.1186/1471-2180-11-36 . free .
- Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E . 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 (BBA) - General Subjects . 1840 . 1 . 535–44 . January 2014 . 24128931 . 10.1016/j.bbagen.2013.10.010 . 2108/89370 . free .
- Petrarca P, Ammendola S, Pasquali P, Battistoni A . 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 . March 2010 . 20097857 . 2832539 . 10.1128/jb.01310-09 .
- Blindauer CA . Advances in the molecular understanding of biological zinc transport . Chemical Communications . 51 . 22 . 4544–63 . March 2015 . 25627157 . 10.1039/c4cc10174j . free .
