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 previously devised a strategy (metal-directed protein self-assembly, MDPSA) that utilizes the simultaneous stability, lability, and directionality of metal-ligand bonds to drive protein-protein interactions. Here we show that both the structural and functional scopes of MDPSA can be broadened by incorporation of non-natural metal-chelating ligands onto protein surfaces. A cytochrome cb(562) variant, MBP-Phen1, which features a covalently attached phenanthroline (Phen) group on its surface, self-assembles into an unusual triangular architecture (Ni(3):MBP-Phen1(3)) upon binding Ni as a result of specific Phen-protein interactions. The crystal structure of Ni(3):MBP-Phen1(3) reveals that the Phen group is buried in a small pocket on the protein surface, which results in an unsaturated Ni coordination environment.
A superprotein triangle driven by nickel(II) coordination: exploiting non-natural metal ligands in protein self-assembly.,Radford RJ, Tezcan FA J Am Chem Soc. 2009 Jul 8;131(26):9136-7. PMID:19527025[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Radford RJ, Tezcan FA. A superprotein triangle driven by nickel(II) coordination: exploiting non-natural metal ligands in protein self-assembly. J Am Chem Soc. 2009 Jul 8;131(26):9136-7. PMID:19527025 doi:10.1021/ja9000695
