3FOP

A Triangular Cytochrome b562 Superstructure Mediated by Ni Coordination - Hexagonal Form

Summary for 3FOP

• Entry DOI: 10.2210/pdb3fop/pdb
• Related: 256B 2QLA 3FOO
• Descriptor: Soluble cytochrome b562, PROTOPORPHYRIN IX CONTAINING FE, N-1,10-phenanthrolin-5-ylacetamide, ... (5 entities in total)
• Functional Keywords: four helix bundle, electron transport, heme, iron, metal-binding, periplasm, transport
• Biological source: Escherichia coli
• Cellular location: Periplasm: P0ABE7
• Total number of polymer chains: 2
• Total formula weight: 25018.19

Authors

Tezcan, F.A.,Radford, R.J. (deposition date: 2008-12-30, release date: 2009-07-14, Last modification date: 2023-09-06)

Primary citation

Radford, R.J.,Tezcan, F.A.
A superprotein triangle driven by nickel(II) coordination: exploiting non-natural metal ligands in protein self-assembly.
J.Am.Chem.Soc., 131:9136-9137, 2009

PubMed Abstract: We previously devised a strategy (metal-directed protein self-assembly, MDPSA) that utilizes the simultaneous stability, lability, and directionality of metal-ligand bonds to drive protein-protein interactions. Here we show that both the structural and functional scopes of MDPSA can be broadened by incorporation of non-natural metal-chelating ligands onto protein surfaces. A cytochrome cb(562) variant, MBP-Phen1, which features a covalently attached phenanthroline (Phen) group on its surface, self-assembles into an unusual triangular architecture (Ni(3):MBP-Phen1(3)) upon binding Ni as a result of specific Phen-protein interactions. The crystal structure of Ni(3):MBP-Phen1(3) reveals that the Phen group is buried in a small pocket on the protein surface, which results in an unsaturated Ni coordination environment.

PubMed: 19527025
DOI: 10.1021/ja9000695

Experimental method

X-RAY DIFFRACTION (3 Å)