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      Crystal structure of an inferred ancestral bacterial pyruvate decarboxylase

      Buddrus, Lisa; Andrews, Emma Sophie Vout; Leak, David J.; Danson, Michael J.; Arcus, Vickery L.; Crennell, Susan J.
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      2018 buddrus andrews leak danson arcus crennell Acta Crystallographica Section F.pdf
      Published version, 811.8Kb
      DOI
       10.1107/S2053230X18002819
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      Buddrus, L., Andrews, E. S. V., Leak, D. J., Danson, M. J., Arcus, V. L., & Crennell, S. J. (2018). Crystal structure of an inferred ancestral bacterial pyruvate decarboxylase. Acta Crystallographica Section F: Structural Biology Communications, 74, 179–186. https://doi.org/10.1107/S2053230X18002819
      Permanent Research Commons link: https://hdl.handle.net/10289/11883
      Abstract
      Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a key enzyme in homofermentative metabolism where ethanol is the major product. PDCs are thiamine pyrophos­phate- and Mg2+ ion-dependent enzymes that catalyse the non-oxidative decarboxylation of pyruvate to acetaldehyde and carbon dioxide. As this enzyme class is rare in bacteria, current knowledge of bacterial PDCs is extremely limited. One approach to further the understanding of bacterial PDCs is to exploit the diversity provided by evolution. Ancestral sequence reconstruction (ASR) is a method of computational molecular evolution to infer extinct ancestral protein sequences, which can then be synthesized and experimentally characterized. Through ASR a novel PDC was generated, designated ANC27, that shares only 78% amino-acid sequence identity with its closest extant homologue (Komagataeibacter medellinensis PDC, GenBank accession No. WP_014105323.1), yet is fully functional. Crystals of this PDC diffracted to 3.5 Å resolution. The data were merged in space group P3221, with unit-cell parameters a = b = 108.33, c = 322.65 Å, and contained two dimers (two tetramer halves) in the asymmetric unit. The structure was solved by molecular replacement using PDB entry 2wvg as a model, and the final R values were Rwork = 0.246 (0.3671 in the highest resolution bin) and Rfree = 0.319 (0.4482 in the highest resolution bin). Comparison with extant bacterial PDCs supports the previously observed correlation between decreased tetramer interface area (and number of interactions) and decreased thermostability.
      Date
      2018
      Type
      Journal Article
      Publisher
      International Union of Crystallography
      Rights
      This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
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      • Science and Engineering Papers [3019]
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