Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

A taste of copper

¹Department of Biological Structure, University of Washington, Seattle 98195-7420, USA.

Nature Structural Biology

|November 1, 1995

Summary

New protein structures reveal copper

Related Experiment Videos

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

Arginine-140 and isoleucine-141 determine the 17beta-estradiol-binding specificity of the sex-steroid-binding protein (SBP, or SHBG) of human plasma.

Protein science : a publication of the Protein Society·2001

Same author

Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y.

Proteins·2000

Same author

Molecular architecture of the mutagenic active site of human immunodeficiency virus type 1 reverse transcriptase: roles of the beta 8-alpha E loop in fidelity, processivity, and substrate interactions.

Biochemistry·2000

Same author

Thermus aquaticus DNA polymerase I mutants with altered fidelity. Interacting mutations in the O-helix.

The Journal of biological chemistry·2000

Same author

Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms.

The Journal of biological chemistry·2000

Same author

New human immunodeficiency virus, type 1 reverse transcriptase (HIV-1 RT) mutants with increased fidelity of DNA synthesis. Accuracy, template binding, and processivity.

The Journal of biological chemistry·1999

Area of Science:

Biochemistry
Structural Biology
Bioinorganic Chemistry

Background:

Copper proteins play crucial roles in biological electron transfer.
Understanding protein structure is key to elucidating function.
Cytochrome oxidase and amine oxidase are vital copper-containing enzymes.

Framework:

Novel crystal structures of copper proteins were determined.
The study focused on cupredoxin-like folds and a new fold for amine oxidase.
Computational analysis was used to predict and confirm structural features.

Implementation:

X-ray crystallography was employed to resolve new protein structures.
Structural comparisons were made to existing cupredoxin-like proteins.
Electron transfer pathways in cytochrome oxidase were mapped.
The novel fold of amine oxidase was characterized.

Implications:

Confirms predictions regarding copper protein structures.
Elucidates electron transfer mechanisms in cytochrome oxidase.
Reveals a novel function of copper in amine oxidase cofactor formation.
Advances understanding of bioinorganic chemistry and enzyme mechanisms.