3C63

Tetrameric Cytochrome cb562 (K34/H59/D62/H63/H73/A74/H77) Assembly Stabilized by Interprotein Zinc Coordination

Summary for 3C63

• Entry DOI: 10.2210/pdb3c63/pdb
• Related: 2BC5 2QLA 3C62
• Descriptor: Soluble cytochrome b562, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: 16-helix bundle, interfacial zn-coordination, electron transport, heme, iron, metal-binding, transport
• Biological source: Escherichia coli
• Cellular location: Periplasm : P0ABE7
• Total number of polymer chains: 4
• Total formula weight: 49376.06

Authors

Tezcan, F.A.,Salgado, E.N.,Lewis, R.A.,Faraone-Mennella, J. (deposition date: 2008-02-02, release date: 2008-05-06, Last modification date: 2023-08-30)

Primary citation

Salgado, E.N.,Lewis, R.A.,Faraone-Mennella, J.,Tezcan, F.A.
Metal-mediated self-assembly of protein superstructures: influence of secondary interactions on protein oligomerization and aggregation.
J.Am.Chem.Soc., 130:6082-6084, 2008

PubMed Abstract: We have previously demonstrated that non-self-associating protein building blocks can oligomerize to form discrete supramolecular assemblies under the control of metal coordination. We show here that secondary interactions (salt bridges and hydrogen bonds) can be critical in guiding the metal-induced self-assembly of proteins. Crystallographic and hydrodynamic measurements on appropriately engineered cytochrome cb562 variants pinpoint the importance of a single salt-bridging arginine side chain in determining whether the protein monomers form a discrete Zn-induced tetrameric complex or heterogeneous aggregates. The combined ability to direct PPIs through metal coordination and secondary interactions should provide the specificity required for the construction of complex protein superstructures and the selective control of cellular processes that involve protein-protein association reactions.

PubMed: 18422313
DOI: 10.1021/ja8012177

Experimental method

X-RAY DIFFRACTION (1.75 Å)