3de9
Crystal Structure of a Trimeric Cytochrome cb562 Assembly Induced by Nickel CoordinationCrystal Structure of a Trimeric Cytochrome cb562 Assembly Induced by Nickel Coordination
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 PubMedWe 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 AlsoReferences
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