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. 2013 Feb 19;110(10):3829–3834. doi: 10.1073/pnas.1217306110

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Fig. 4. — Removal of the conserved H120–H43–T39 linkage by mutation H43F. (A) X-ray structures of apoSOD1^ΔIVΔVII (PDB entry 4BCZ) and apo (PDB entry 4BD4) show that H43F leads to relaxation of the twisted backbone carbonyl of H120 into the sheet where it H-bonds to the amide of G44. (B) Cu²⁺ coordination twists back the carbonyl of H120 into the core, forcing the protein into a native-like metal-binding geometry. Holo (PDB entry 4BCZ).

Inline graphic — Removal of the conserved H120–H43–T39 linkage by mutation H43F. (A) X-ray structures of apoSOD1^ΔIVΔVII (PDB entry 4BCZ) and apo (PDB entry 4BD4) show that H43F leads to relaxation of the twisted backbone carbonyl of H120 into the sheet where it H-bonds to the amide of G44. (B) Cu²⁺ coordination twists back the carbonyl of H120 into the core, forcing the protein into a native-like metal-binding geometry. Holo (PDB entry 4BCZ).