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Crystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination MotifCrystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination Motif
Structural highlights
FunctionC562_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 PubMedProtein homodimerization is the simplest form of oligomerization that is frequently utilized for the construction of functional biological assemblies and the regulation of cellular pathways. Despite its simplicity, dimerization still poses an enormous challenge for protein engineering and chemical maniupulation, owing to the large molecular surfaces involved in this process. We report here the construction of a hybrid coordination motif-consisting of a natural (His) and a non-natural ligand (quinolate)-on the alpha-helical surface of cytochrome cb(562), which (a) simultaneously binds divalent metals with high affinity, (b) leads to a metal-induced increase in global protein stability, and importantly, (c) enables the formation of a discrete protein dimer, whose shape is dictated by the inner-sphere metal coordination geometry and closely approximates that of the DNA-binding domains of bZIP family transcription factors. Controlled Protein Dimerization through Hybrid Coordination Motifs.,Radford RJ, Nguyen PC, Ditri TB, Figueroa JS, Tezcan FA Inorg Chem. 2010 May 3;49(9):4362-9. PMID:20377257[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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