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      Crystal structure of pyruvate decarboxylase from Zymobacter palmae

      Buddrus, Lisa; Andrews, Emma Sophie Vout; Leak, David J.; Danson, Michael J.; Arcus, Vickery L.; Crennell, Susan J.
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      Crystal structure article 2016.pdf
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      DOI
       10.1107/S2053230X16012012
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      Buddrus, L., Andrews, E. S. V., Leak, D. J., Danson, M. J., Arcus, V. L., & Crennell, S. J. (2016). Crystal structure of pyruvate decarboxylase from Zymobacter palmae. Acta Crystallographica Section F-Structural Biology Communications, 72, 700–706. https://doi.org/10.1107/S2053230X16012012
      Permanent Research Commons link: https://hdl.handle.net/10289/11037
      Abstract
      Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a thiamine pyrophosphate- and Mg²⁺ ion-dependent enzyme that catalyses the non-oxidative decarboxylation of pyruvate to acetaldehyde and carbon dioxide. It is rare in bacteria, but is a key enzyme in homofermentative metabolism, where ethanol is the major product. Here, the previously unreported crystal structure of the bacterial pyruvate decarboxylase from Zymobacter palmae is presented. The crystals were shown to diffract to 2.15 Å resolution. They belonged to space group P21, with unit-cell parameters a = 204.56, b = 177.39, c = 244.55 Å and Rᵣ.ᵢ.ₘ. = 0.175 (0.714 in the highest resolution bin). The structure was solved by molecular replacement using PDB entry 2vbi as a model and the final R values were Rwₒᵣₖ = 0.186 (0.271 in the highest resolution bin) and Rfᵣₑₑ = 0.220 (0.300 in the highest resolution bin). Each of the six tetramers is a dimer of dimers, with each monomer sharing its thiamine pyrophosphate across the dimer interface, and some contain ethylene glycol mimicking the substrate pyruvate in the active site. Comparison with other bacterial PDCs shows a correlation of higher thermostability with greater tetramer interface area and number of interactions.
      Date
      2016
      Type
      Journal Article
      Publisher
      International Union of Crystallography
      Rights
      This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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