Uncovering the Transmembrane Metal Binding Site of the Novel Bacterial Major Facilitator Superfamily-Type Copper Importer CcoA

MBio
Bahia Khalfaoui-HassaniFevzi Daldal

Abstract

Uptake and trafficking of metals and their delivery to their respective metalloproteins are important processes. Cells need precise control of each step to avoid exposure to excessive metal concentrations and their harmful consequences. Copper (Cu) is a required micronutrient used as a cofactor in proteins. However, in large amounts, it can induce oxidative damage; hence, Cu homeostasis is indispensable for cell survival. Biogenesis of respiratory heme-Cu oxygen (HCO) reductases includes insertion of Cu into their catalytic subunits to form heme-Cu binuclear centers. Previously, we had shown that CcoA is a major facilitator superfamily (MFS)-type bacterial Cu importer required for biogenesis of cbb3-type cytochrome c oxidase (cbb3-Cox). Here, using Rhodobacter capsulatus, we focused on the import and delivery of Cu to cbb3-Cox. By comparing the CcoA amino acid sequence with its homologues from other bacterial species, we located several well-conserved Met, His, and Tyr residues that might be important for Cu transport. We determined the topology of the transmembrane helices that carry these residues to establish that they are membrane embedded, and substituted for them amino acids that do not ligand metal atoms. Characterizatio...Continue Reading

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Citations

Oct 2, 2019·Proceedings of the National Academy of Sciences of the United States of America·Dorian MarckmannHans-Georg Koch
Mar 10, 2020·Metallomics : Integrated Biometal Science·Nur SelamogluFevzi Daldal
Feb 6, 2019·Scientific Reports·Yang ZhangBahia Khalfaoui-Hassani
Sep 24, 2020·Membranes·Andreea AndreiHans-Georg Koch

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Methods Mentioned

BETA
PCR

Software Mentioned

TMRPres2D

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