3DE8

Crystal Structure of a Dimeric Cytochrome cb562 Assembly Induced by Copper Coordination

Summary for 3DE8

Entry DOI	10.2210/pdb3de8/pdb
Related	2BC5 2QLA 3DE9
Descriptor	Soluble cytochrome b562, COPPER (II) ION, CALCIUM ION, ... (5 entities in total)
Functional Keywords	cu-stabilized dimeric superstructure, electron transport, heme, iron, metal-binding, periplasm, transport, metal binding protein
Biological source	Escherichia coli
Cellular location	Periplasm: P0ABE7
Total number of polymer chains	4
Total formula weight	49865.21
Authors	Salgado, E.N.,Lewis, R.A.,Rheingold, A.L.,Tezcan, F.A. (deposition date: 2008-06-08, release date: 2009-04-21, Last modification date: 2024-02-21)
Primary citation	Salgado, E.N.,Lewis, R.A.,Mossin, S.,Rheingold, A.L.,Tezcan, F.A. Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination. Inorg.Chem., 48:2726-2728, 2009 Cited by PubMed Abstract: We describe the metal-dependent self-assembly of symmetrical protein homooligomers from protein building blocks that feature appropriately engineered metal-chelating motifs on their surfaces. Crystallographic studies indicate that the same four-helix-bundle protein construct, MBPC-1, can self-assemble into C(2) and C(3) symmetrical assemblies dictated by Cu(II) and Ni(II) coordination, respectively. The symmetry inherent in metal coordination can thus be directly applied to biological self-assembly. PubMed: 19267481 DOI: 10.1021/ic9001237 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.72 Å)

Structure validation