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Verdecia M.A., Larkin R.M., Ferrer J.L., Riek R., Chory J., and Noel J.P. Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding. PLoS Biol 3 (2005) e151. GUN4 is a novel porphyrin-binding protein that dramatically enhances the activity of MgCh. GUN4 also plays a role in both photoprotection and the cellular shuttling of tetrapyrroles. The authors reported a crystal structure for Synechocystis GUN4. They also presented data from biophysical and biochemical analyses revealing the specific site of interaction between GUN4 and MgCh. Their data indicate a novel protective function for GUN4 in tetrapyrrole trafficking. The combined structural and energetic analyses presented in this paper form the physical-chemical basis for understanding GUN4 biological activity, including its roles both in the stimulation of Mg-chelatase activity and in Mg-Proto IX retrograde signaling.
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