A Charge-reversal Point Mutation Completely Depletes Flavin Chromophore from European Robin Cryptochrome 4a Protein

Authors:
Preprint
Publisher website
Google Scholar
Abstract
Cryptochrome 4a (Cry4a) is a magnetically sensitive protein that could enable night-migratory birds to sense the geomagnetic field for navigation. The key to the protein magnetic sensitivity is the flavin adenine dinucleotide (FAD) cofactor, which initiates the electron transfer within the protein leading to a spin-correlated radical pair. De-spite its importance, the mechanism of FAD binding in avian Cry4a proteins remains unclear. Here we show that point mutagenesis of positively charged arginine residue at position 356 to negatively charged glutamic acid completely depletes FAD binding from European robin ( Erithacus rubecula ) Cry4a. The result indicates that electrostatic in-teractions constitute the primary driving force that enables FAD binding in European robin Cry4a. The finding provides new structural insight into the molecular basis of FAD binding in Cry4 and advances our understanding on the biophysical underpinnings of bird magnetoreception. Table of Contents Graphic:
All Related Versions
Funding Information
  • Novo Nordisk Fonden (NNF20OC0061575)
  • European Research Council (810002)
  • Volkswagen Foundation (Lichtenberg Professorship)
  • Deutsche Forschungsgemeinschaft (395940726)
  • Deutsche Forschungsgemeinschaft (533653176)
  • Deutsche Forschungsgemeinschaft (514664767)
  • Niedersächsisches Ministerium für Wissenschaft und Kultur

This publication has 45 references indexed in Scilit: