2qla
From Proteopedia
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Crystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 Molecules
Overview
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 cb562, 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 cb562 are, governed entirely by metal coordination without significant thermodynamic, bias from specific PPIs.
About this Structure
2QLA is a Single protein structure of sequence from Escherichia coli with and as ligands. Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.
Reference
Controlling Protein-Protein Interactions through Metal Coordination: Assembly of a 16-Helix Bundle Protein., Salgado EN, Faraone-Mennella J, Tezcan FA, J Am Chem Soc. 2007 Nov 7;129(44):13374-5. Epub 2007 Oct 12. PMID:17929927
Page seeded by OCA on Thu Jan 31 10:58:54 2008
