# Structural and functional characterization of putative Cu importer CopD

> **NIH NIH F32** · NORTHWESTERN UNIVERSITY · 2022 · $28,521

## Abstract

Project Summary/Abstract
 Copper is an essential metal ion for all organisms, including prokaryotes. Strict control of
copper homeostasis is maintained using a suite of copper-binding and transporting proteins. The
transmembrane protein CopD is implicated in maintaining copper homeostasis by transporting
copper into the bacterial cytoplasm. The molecular basis for cytoplasmic copper import is not
known, and no ortholog of CopD has been studied on the molecular level. In this project, the CopD
protein from Methylosinus trichosporium OB3b will be characterized using a multi-pronged
structural, functional, and genetic approach. We will test the hypothesis that this protein is
involved in import of copper to the cytoplasm and elucidate the molecular basis for function.
Complementary genetic manipulation of the native organism will help determine the role of this
protein in vivo. This research project will elucidate a new paradigm in bacterial copper
homeostasis and broaden our understanding of membrane transporters by providing the first
characterization of a novel family. More broadly, these efforts will lay the foundation for targeting
copper import pathways as an antibiotic strategy.
 This research pursuit will be the main focus of a comprehensive training program aimed
at bolstering many technical skills and interpersonal leadership skills through training in the
Rosenzweig laboratory. Training will be acquired in biochemical, molecular biology, genetic, and
structural biology techniques and will facilitate completion of the research project. Training and
resources provided by the Structural Biology Facility will enable structural investigation using
crystallography and electron microscopy. Training opportunities outside the laboratory, such as
programs at the Life Sciences Collaborative Access Team (LS-CAT) beamlines at the Advanced
Photon Source (APS) at Argonne National Laboratory, will also be available. All of the necessary
equipment is available in the Departments of Molecular Biosciences and Chemistry at
Northwestern University with easy access to the beamlines at the APS. In addition, collaborations
with the Hoffman laboratory for electron paramagnetic resonance (EPR) spectroscopy, the He
laboratory for cryogenic electron microscopy, and the Lewinson laboratory for metal transport
assays will facilitate successful completion of this research. This multi-faceted training program
combined with the collaborative and scientific environment at Northwestern University will provide
excellent interdisciplinary training for an independent academic position.

## Key facts

- **NIH application ID:** 10330998
- **Project number:** 5F32GM140573-02
- **Recipient organization:** NORTHWESTERN UNIVERSITY
- **Principal Investigator:** Rose Currier Hadley
- **Activity code:** F32 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2022
- **Award amount:** $28,521
- **Award type:** 5
- **Project period:** 2021-07-01 → 2022-11-25

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10330998

## Citation

> US National Institutes of Health, RePORTER application 10330998, Structural and functional characterization of putative Cu importer CopD (5F32GM140573-02). Retrieved via AI Analytics 2026-05-22 from https://api.ai-analytics.org/grant/nih/10330998. Licensed CC0.

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