Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination.
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.
Salgado
Eric N
EN
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093, USA.
Lewis
Richard A
RA
Mossin
Susanne
S
Rheingold
Arnold L
AL
Tezcan
F Akif
FA
D003300:Copper / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry*; D009942:Organometallic Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D015032:Zinc / Q000737:chemistry
D008667:Metalloproteins; D009942:Organometallic Compounds; D003300:Copper; D009532:Nickel; D015032:Zinc