Faiella Marina, Andreozzi Concetta, de Rosales Rafael Torres Martin, Pavone Vincenzo, Maglio Ornella, Nastri Flavia, DeGrado William F, Lombardi Angela
Department of Chemistry, University Federico II of Napoli, Complesso Universitario Monte S. Angelo, Italy.
Nat Chem Biol. 2009 Dec;5(12):882-4. doi: 10.1038/nchembio.257. Epub 2009 Nov 8.
Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol-binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Sufficient stability was, however, obtained by optimizing the sequence of a loop distant from the active site.
在此，我们报告了一种具有酚氧化酶活性的四螺旋束双铁蛋白的从头设计和核磁共振结构。辅因子结合位点和酚结合位点的引入需要纳入对蛋白质折叠自由能有害的残基。然而，通过优化远离活性位点的一个环的序列，获得了足够的稳定性。
