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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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The fungal zinc metalloenzyme CafD from Aspergillus fumigatus is a minor β-carbonic anhydrase (β-CA) with low CO2 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 (C39A or E54A) 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 C39A 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 E54 and R56 residues of the two chains. By contrast, the E54A 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.
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참고문헌 (24)
참고문헌 신청
Carter, J. M. / 1969 / Electrometric assay of rate of hydration of CO2 for investigation of kinetics of carbonic anhydrase / J Physiol 204:60p~62p
Davis, I. W. / 2007 / MolProbity : all-atom contacts and structure validation for proteins and nucleic acids / Nucleic Acids Res 35:W375~W383
Del Prete, S. / 2014 / Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum-The h-carbonic anhydrases / Bioorg Med Chem Lett 24:4389~4396
Del Prete, S. / 2014 / Cloning, characterization and anion inhibition study of the d-class carbonic anhydrase(TweCA)from the marine diatom Thalassiosira weissflogii / Bioorgan Med Chem 22:531~537
Emsley, P. / 2004 / Coot : model-building tools for molecular graphics / Acta Crystallogr D Biol Crystallogr 60:2126~2132
Davis, I. W. / 2007 / MolProbity : all-atom contacts and structure validation for proteins and nucleic acids / Nucleic Acids Res 35:W375~W383
Del Prete, S. / 2014 / Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum-The h-carbonic anhydrases / Bioorg Med Chem Lett 24:4389~4396
Del Prete, S. / 2014 / Cloning, characterization and anion inhibition study of the d-class carbonic anhydrase(TweCA)from the marine diatom Thalassiosira weissflogii / Bioorgan Med Chem 22:531~537
Emsley, P. / 2004 / Coot : model-building tools for molecular graphics / Acta Crystallogr D Biol Crystallogr 60:2126~2132
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