Structural highlights
Function
[C562_ECOLX] Electron-transport protein of unknown function.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination.,Salgado EN, Lewis RA, Mossin S, Rheingold AL, Tezcan FA Inorg Chem. 2009 Apr 6;48(7):2726-8. PMID:19267481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Salgado EN, Lewis RA, Mossin S, Rheingold AL, Tezcan FA. Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination. Inorg Chem. 2009 Apr 6;48(7):2726-8. PMID:19267481 doi:10.1021/ic9001237
