Copper is an essential micronutrient for all organisms, serving as a cofactor for enzymes involved in respiration and redox homeostasis. However, copper can also be toxic, necessitating careful control of intracellular concentrations. Since prokaryotic copper enzymes are extracytoplasmic, most research has addressed either copper import to the periplasm for enzyme loading or mechanisms of copper resistance, with little focus on the possibility of controlled cytoplasmic copper import. Nevertheless, growing evidence suggests that import to the cytoplasm may be required for loading of some periplasmic copper enzymes. Putative cytoplasmic copper importers include members of the CopD/YcnJ/YebZ family of transmembrane proteins. Genes encoding these proteins are typically found associated with genes encoding periplasmic copper binding proteins, such as CopC proteins as well as other yet-to-be characterized proteins, including members of the DUF2511 family. This NSF-BSF project focuses on elucidating the structure and function of the E. coli proteins YobA (CopC-like), YebZ (putative importer), and YebY (DUF2511 family), encoded by the AZY operon. The proposed research combines genetic, computational, biophysical, and structural approaches and leverages the complementary expertises of the collaborating laboratories in the US and Israel.
|Effective start/end date||1/1/20 → 12/31/23|
- National Science Foundation (MCB-1938715)
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