The E. coli Zur protein in a dimer-of-dimers orientation (blue/light blue and red/orange), interacting with DNA (yellow) and zinc ions (gray spheres). Rendered from PDB: 4MTD.
Identifiers
Organism
Escherichia coli
Symbol
Zur
PDB
4MTD
UniProt
P0AC51
Search for
Structures
Swiss-model
Domains
InterPro
The zinc uptake regulator (Zur) gene is a bacterial gene that codes for a transcription factor protein involved in zinc homeostasis. The protein is a member of the ferric uptake regulator family and binds zinc with high affinity. It typically functions as a repressor of zinc uptake proteins via binding to characteristic promoter DNA sequences in a dimer-of-dimers arrangement that creates strong cooperativity.[1] Under conditions of zinc deficiency, the protein undergoes a conformational change that prevents DNA binding, thereby lifting the repression and causing zinc uptake genes such as ZinT and the ZnuABC zinc transporter to be expressed.[1][2][3]
^ abGilston BA, Wang S, Marcus MD, Canalizo-Hernández MA, Swindell EP, Xue Y, Mondragón A, O'Halloran TV (November 2014). "Structural and mechanistic basis of zinc regulation across the E. coli Zur regulon". PLOS Biology. 12 (11): e1001987. doi:10.1371/journal.pbio.1001987. PMC 4219657. PMID 25369000.
^Blindauer CA (March 2015). "Advances in the molecular understanding of biological zinc transport" (PDF). Chemical Communications. 51 (22): 4544–63. doi:10.1039/c4cc10174j. PMID 25627157.
^Graham AI, Hunt S, Stokes SL, Bramall N, Bunch J, Cox AG, McLeod CW, Poole RK (July 2009). "Severe zinc depletion of Escherichia coli: roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins". The Journal of Biological Chemistry. 284 (27): 18377–89. doi:10.1074/jbc.m109.001503. PMC 2709383. PMID 19377097.
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