Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 49, Pages 21940-21944Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202009226
Keywords
bioinorganic chemistry; metalloproteins; protein design; protein structures; supramolecular chemistry
Categories
Funding
- NSF [CHE1607145]
- NIH (CBI traineeship) [T32GM112584, R01GM138884]
- NASA [80NSSC18M0093]
- DOE, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515, DE-AC02-05CH11231]
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To mimic a hypothetical pathway for protein evolution, we previously tailored a monomeric protein (cyt cb(562)) for metal-mediated self-assembly, followed by re-design of the resulting oligomers for enhanced stability and metal-based functions. We show that a single hydrophobic mutation on the cyt cb(562)surface drastically alters the outcome of metal-directed oligomerization to yield a new trimeric architecture, (TriCyt1)(3.)This nascent trimer was redesigned into second and third-generation variants (TriCyt2)(3)and (TriCyt3)(3)with increased structural stability and preorganization for metal coordination. The three TriCyt variants combined furnish a unique platform to 1) provide tunable coupling between protein quaternary structure and metal coordination, 2) enable the construction of metal/pH-switchable protein oligomerization motifs, and 3) generate a robust metal coordination site that can coordinate all mid-to-late first-row transition-metal ions with high affinity.
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