The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii

Genady Pankovs, Gabriela Mol Avelar, Grant Buchanan, Sarah J. Coulthurst, Bill Hunter (Lead / Corresponding author)

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Abstract

Bacteria exploit specialized secretion systems to assist in competition for resources, in collaboration and in communication. Here, a protocol for the recombinant production, purification and crystallization of a protein linked to the Acinetobacter baumannii type VI secretion system is provided. A high-resolution structure of this trimeric protein is reported, revealing the characteristic dual β-α-β subunit fold typical of longer subunit members of the tautomerase superfamily. The protein does not appear to be toxic to bacteria or yeast under the conditions tested. The possible biological role of this protein is discussed.

Original languageEnglish
Pages (from-to)8-16
Number of pages9
JournalActa Crystallographica Section F: Structural Biology Communications
Volume79
Issue number1
Early online date8 Dec 2022
DOIs
Publication statusPublished - Jan 2023

Keywords

  • Acinetobacter baumannii
  • 4-oxalocrotonate tautomerase
  • tautomerase superfamily
  • type VI secretion system

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