7TEP

Crystal structure of a Cu-bound cytochrome cb562 variant in the presence of reductant

Summary for 7TEP

Entry DOI	10.2210/pdb7tep/pdb
Descriptor	Soluble cytochrome b562, HEME C, COPPER (II) ION, ... (4 entities in total)
Functional Keywords	metalloprotein, assembly, metal binding protein
Biological source	Escherichia coli
Total number of polymer chains	4
Total formula weight	49356.65
Authors	Kakkis, A.,Golub, E. (deposition date: 2022-01-05, release date: 2022-06-29, Last modification date: 2023-10-25)
Primary citation	Kakkis, A.,Golub, E.,Choi, T.S.,Tezcan, F.A. Redox- and metal-directed structural diversification in designed metalloprotein assemblies. Chem.Commun.(Camb.), 58:6958-6961, 2022 Cited by PubMed Abstract: Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown - through extensive structural and biophysical characterization - to access five distinct oligomeric states, exemplifying how the complex interplay between hydrophobic, metal-ligand, and reversible covalent interactions could be harnessed to obtain multiple, responsive protein architectures from a single building block. PubMed: 35642584 DOI: 10.1039/d2cc02440c PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation