Copper homeostasis protein: Difference between revisions

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<StructureSection load='3iwp' size='350' side='right' caption='Human copper homeostasis protein CutC (PDB entry [[3iwp]])' scene=''>
<StructureSection load='3iwp' size='350' side='right' caption='Human copper homeostasis protein CutC (PDB entry [[3iwp]])' scene=''>


'''Copper homeostasis proteins''' are responsible for regulation of copper concentration in the cell in order to avoid toxicity caused by high concentration of the metal.<ref>PMID:19878721</ref>  For details on CsoR see [[Molecular Playground/CsoR and RcnR]].
'''Copper homeostasis proteins''' are responsible for regulation of copper concentration in the cell in order to avoid toxicity caused by high concentration of the metal.<ref>PMID:19878721</ref> '''Copper homeostasis protein CutE''' is called '''apolipoprotein N-acyltransferase'''. For details on CsoR see [[Molecular Playground/CsoR and RcnR]].
</StructureSection>
</StructureSection>



Revision as of 11:27, 9 February 2025


Copper homeostasis proteins are responsible for regulation of copper concentration in the cell in order to avoid toxicity caused by high concentration of the metal.[1] Copper homeostasis protein CutE is called apolipoprotein N-acyltransferase. For details on CsoR see Molecular Playground/CsoR and RcnR.

Human copper homeostasis protein CutC (PDB entry 3iwp)

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3D Structures of copper homeostasis protein3D Structures of copper homeostasis protein

Updated on 09-February-2025

1x7i, 1x8c, 1twd – CutC + Ca – Shigella flexneri
2z4h, 2z4i – CutF (mutant) – Escherichia coli
3iwp – CutC – human
4r9x – CutC – Bacillus anthracis
2bdq – CutC – Streptococcus agalactiae
3aai – CsoR – Thermus thermophilus
2hh7 – CsoR + Cu – Mycobacterium tuberculosis

ReferencesReferences

  1. Li Y, Du J, Zhang P, Ding J. Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site. J Struct Biol. 2010 Mar;169(3):399-405. doi: 10.1016/j.jsb.2009.10.012. Epub 2009, Oct 28. PMID:19878721 doi:http://dx.doi.org/10.1016/j.jsb.2009.10.012

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Michal Harel, Alexander Berchansky, Jaime Prilusky