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

doi:10.1107/S2053230X22011414

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 language	English
Pages (from-to)	8-16
Number of pages	9
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	79
Issue number	1
Early online date	8 Dec 2022
DOIs	https://doi.org/10.1107/S2053230X22011414
Publication status	Published - Jan 2023

Keywords

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

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10.1107/S2053230X22011414Licence: CC BY

Final Published VersionFinal published version, 1.3 MBLicence: CC BY

Cite this

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

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.",

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AB - 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.

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

Abstract

Keywords

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Targeting a New Kingdom The Nature and Importance of Type VI Secretion System Mediated Anti Fungal Activity (joint with University of Newcastle, Heriot-Watt University, Hans Knoll Institute, University of Exeter)

State-of-the-Art Facilities for Structural Biology at the University of Dundee

Cite this

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Projects

Targeting a New Kingdom The Nature and Importance of Type VI Secretion System Mediated Anti Fungal Activity (joint with University of Newcastle, Heriot-Watt University, Hans Knoll Institute, University of Exeter)

State-of-the-Art Facilities for Structural Biology at the University of Dundee

Cite this