5EIL : Computational design of a high-affinity metalloprotein homotrimer containing a metal chelating non-canonical amino acid

  • Jeremy Mills (Contributor)
  • José Henrique Pereira (Contributor)
  • Banumathi Sankaran (Contributor)
  • Peter H. Zwart (Contributor)
  • David Baker (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Classification:DE NOVO PROTEIN
Release Date:2016-11-16
Deposition Date:2015-10-30
Revision Date:2017-01-18#2017-09-27
Molecular Weight:50987.46
Macromolecule Type:Protein
Residue Count:477
Atom Site Count:3588

Metal-chelating heteroaryl small molecules have found widespread use as building blocks for coordination-driven, self-assembling nanostructures. The metal-chelating noncanonical amino acid (2,2'-bipyridin-5yl)alanine (Bpy-ala) could, in principle, be used to nucleate specific metalloprotein assemblies if introduced into proteins such that one assembly had much lower free energy than all alternatives. Here we describe the use of the Rosetta computational methodology to design a self-assembling homotrimeric protein with [Fe(Bpy-ala)
Date made available2016

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