Crystal structure of pyruvate decarboxylase from Zymobacter palmae

Lisa Buddrus, Emma S. V. Andrews, David J. Leak, Michael J. Danson, Vickery L. Arcus, Susan J. Crennell

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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 2.15Å resolution. They belonged to space group P21, with unit-cell parameters a = 204.56, b = 177.39, c = 244.55Å 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.
Original languageEnglish
Pages (from-to)700-706
JournalActa Crystallographica Section F:Structural Biology Communications
Volume72
Issue number9
DOIs
Publication statusPublished - 1 Sep 2016

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