Research Repository

Copper Storage Protein From Streptomyces Lividans

Worrall, Jonathan AR (2021) 'Copper Storage Protein From Streptomyces Lividans.' In: Scott, Robert A, (ed.) Encyclopedia of Inorganic and Bioinorganic Chemistry (EIBC). Wiley. ISBN 9781119951438

[img]
Preview
Text
9781119951438.eibc2777.pdf - Published Version

Download (2MB) | Preview

Abstract

The ability of copper to cycle between two redox states (CuI/CuII), each having a preference for either soft or hard ligands, gives rise to a diverse spectrum of coordination spheres within protein scaffolds that results in a broad range of functionalities. Maintaining cellular copper bioavailability and preventing the detrimental effects associated with excess CuI is critical for cell viability. In the bacterial cytosol, regulatory systems exist that are chemically tuned to constrain and regulate cuprous ion bioavailability through high-affinity-binding sites that use predominately cuprous-thiolate coordination chemistry. Recently, a family of four-helix bundle proteins with a cysteine-rich core has been discovered to reside in the bacterial cytosol. These proteins have been named copper storage proteins (Csps), reflecting their ability to coordinate up to 20 cuprous ions in the cysteine-rich core. In the Gram-positive, filamentous bacterium, Streptomyces lividans, a Csp is present. The copper regulatory systems in S. lividans have been well studied and the extracytoplasmic copper-trafficking pathways, essential to initiate the copper-dependent morphological differentiation, identified. The role the Csp plays in the copper biochemistry of S. lividans has been investigated from both a biological and bioinorganic chemistry perspective, and the current understanding is summarized.

Item Type: Book Section
Additional Information: Encyclopedia of Inorganic and Bioinorganic Chemistry, Online © 2011–2021 John Wiley & Sons, Ltd. This article is © 2021 John Wiley & Sons, Ltd. This article was published in the Encyclopedia of Inorganic and Bioinorganic Chemistry in 2021 by John Wiley & Sons, Ltd. DOI: 10.1002/9781119951438.eibc2777
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Elements
Date Deposited: 02 Jul 2021 11:55
Last Modified: 02 Jul 2021 11:55
URI: http://repository.essex.ac.uk/id/eprint/30691

Actions (login required)

View Item View Item