Work

Controlling Protein−Protein Interactions through Metal Coordination: Assembly of a 16-Helix Bundle Protein

Year: 2007

Type: article

Abstract: The prediction, design, and control of protein−protein interactions (PPIs) remain great challenges despite recent advances. Here we describe the chemical control of PPIs through the use of metal coordination, which circumvents the requirement of PPIs for an extensive set of weak interactions spread over a large surface. A non-self-associating four-bundle protein, cytochrome cb 562, with appropriately engineered metal-binding motifs self-assembles to a 16-helix quaternary structure upon addition of equimolar Zn. The crystal structure of the assembly, combined with PFG diffusion NMR and sedimentation velocity experiments, indicates that the oligomerization properties of cytochrome cb 562 are governed entirely by metal coordination without significant thermodynamic bias from specific PPIs.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja075261o

Authors: Eric N. Salgado, Jasmin Faraone-Mennella, F. Akif Tezcan

Institution: University of California San Diego

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Center for Research Resources

Award: A Synchroton Radiation Structural Biology Resource