Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Helping copper find a home.

T L Poulos1

  • 1Department of Molecular Biology, Program in Macromolecular Structure,

Nature Structural Biology
|July 30, 1999
PubMed
Summary
This summary is machine-generated.

The crystal structure of the superoxide dismutase copper chaperone reveals how it transports copper. This finding is crucial for understanding cellular copper balance and related diseases.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy.

Biochemistry·2008
Same author

Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases.

Journal of inorganic biochemistry·2002
Same author

Substrate recognition sites in 14alpha-sterol demethylase from comparative analysis of amino acid sequences and X-ray structure of Mycobacterium tuberculosis CYP51.

Journal of inorganic biochemistry·2001
Same author

Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism.

Biochemistry·2001
Same author

Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases.

Biochemistry·2001
Same author

Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1.

Biochemistry·2001
Same journal

Fingering nucleic acids: the RNA did it.

Nature structural biology·2003
Same journal

Histone H1.2 as a trigger for apoptosis.

Nature structural biology·2003
Same journal

Tom40: more than just a channel.

Nature structural biology·2003
Same journal

Announcing the worldwide Protein Data Bank.

Nature structural biology·2003
Same journal

Small RNAs come of age.

Nature structural biology·2003
Same journal

Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.

Nature structural biology·2003
See all related articles

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Copper is an essential trace element vital for various cellular processes.
  • Superoxide dismutase copper chaperone (CCS) plays a critical role in delivering copper to superoxide dismutase (SOD).
  • Dysregulation of copper homeostasis is implicated in neurodegenerative diseases and cancer.

Discussion:

  • The determined crystal structure of CCS offers a detailed atomic-level view of the protein.
  • This structure elucidates the binding sites and conformational changes involved in copper transfer.
  • Analysis reveals specific amino acid residues critical for copper coordination and chaperone function.

Key Insights:

  • The crystal structure provides unprecedented insights into the molecular mechanism of copper trafficking by CCS.

Related Experiment Videos

  • It highlights how CCS binds, stabilizes, and delivers copper ions to its target enzyme.
  • Structural data illuminates potential targets for therapeutic intervention in diseases associated with copper dysmetabolism.

    • Outlook:

    • Further structural studies under different conditions will refine our understanding of CCS dynamics.
    • Investigating CCS interactions with other proteins involved in copper metabolism.
    • Exploring the therapeutic potential of targeting CCS in copper-related disorders.