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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.
|Number of pages||9|
|Journal||Acta Crystallographica Section F: Structural Biology Communications|
|Early online date||8 Dec 2022|
|Publication status||Published - Jan 2023|
- Acinetobacter baumannii
- 4-oxalocrotonate tautomerase
- tautomerase superfamily
- type VI secretion system
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State-of-the-Art Facilities for Structural Biology at the University of Dundee
Hunter, B., Lilley, D., Owen-Hughes, T., Wyatt, P. & van Aalten, D.
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