저자 명 : Songwon Kim , Na Jin Kim , Subin Kim , Semi Hong , Jongmin Sung , Mi Sun Jin 
 간행물 정보 : 『 Biodesign 』 7 권 4 호 , 84 ~ 89 쪽 , 전체 6 쪽 
 Songwon Kim , Na Jin Kim , Subin Kim , Semi Hong , Jongmin Sung , Mi Sun Jin . ( 2019 ) . Structural analysis of the non - catalytic zinc binding site in the minor β - carbonic anhydrase CafD . Biodesign , 7 ( 4 ) , 84 - 89 . 
 Songwon Kim , Na Jin Kim , Subin Kim , Semi Hong , Jongmin Sung , Mi Sun Jin . " Structural analysis of the non - catalytic zinc binding site in the minor β - carbonic anhydrase CafD . " Biodesign , 7 . 4 ( 2019 ) : 84 - 89 . 
 The fungal zinc metalloenzyme CafD from Aspergillus fumigatus is a minor β - carbonic anhydrase ( β - CA ) with low CO 2 hydration activity . X - ray crystallography revealed that CafD forms a homodimer that possesses a zinc binding site in the dimer interface in addition to the catalytic zinc in the active … 
 The fungal zinc metalloenzyme CafD from Aspergillus fumigatus is a minor β - carbonic anhydrase ( β - CA ) with low CO 2 hydration activity . X - ray crystallography revealed that CafD forms a homodimer that possesses a zinc binding site in the dimer interface in addition to the catalytic zinc in the active site . However , the role of this ‘ non - catalytic zinc ’ has not been elucidated . In this study , we generated single ( C 39 A or E 54 A ) mutants targeting residues that form the non - catalytic zinc coordination sphere of CafD , and analyzed their structural and biochemical characteristics . Contrary to our expectations , these mutations strongly destabilized the three - dimensional fold of CafD , but the native homodimeric assembly was maintained even though the non - catalytic zinc binding site was disrupted . In the C 39 A mutant , the absence of the noncatalytic zinc permits flipping of a peptide bond , creating extra space for two water molecules that are vital in the formation of a water - mediated hydrogen bond network with the equivalent E 54 and R 56 residues of the two chains . By contrast , the E 54 A mutant contains an unexpected disulfide bond formed between the equivalent cysteine residues at position 39 , which confers stability to the non - catalytic zinc - deficient CafD . Overall , our results demonstrate that a water - mediated hydrogen bond network and a disulfide bond may compensate for the loss of non - catalytic zinc at the dimer interface of CafD , and thereby contribute to structural integrity and / or thermal stability .