Cargando…

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

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 h...

Descripción completa

Detalles Bibliográficos
Autores principales: Pankov, Genady, Mol Avelar, Gabriela, Buchanan, Grant, Coulthurst, Sarah J., Hunter, William N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9813972/
https://www.ncbi.nlm.nih.gov/pubmed/36598351
http://dx.doi.org/10.1107/S2053230X22011414
_version_ 1784864031326076928
author Pankov, Genady
Mol Avelar, Gabriela
Buchanan, Grant
Coulthurst, Sarah J.
Hunter, William N.
author_facet Pankov, Genady
Mol Avelar, Gabriela
Buchanan, Grant
Coulthurst, Sarah J.
Hunter, William N.
author_sort Pankov, Genady
collection PubMed
description 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.
format Online
Article
Text
id pubmed-9813972
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher International Union of Crystallography
record_format MEDLINE/PubMed
spelling pubmed-98139722023-01-09 The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii Pankov, Genady Mol Avelar, Gabriela Buchanan, Grant Coulthurst, Sarah J. Hunter, William N. Acta Crystallogr F Struct Biol Commun Research Communications 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. International Union of Crystallography 2023-01-01 /pmc/articles/PMC9813972/ /pubmed/36598351 http://dx.doi.org/10.1107/S2053230X22011414 Text en © Genady Pankov et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Communications
Pankov, Genady
Mol Avelar, Gabriela
Buchanan, Grant
Coulthurst, Sarah J.
Hunter, William N.
The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii
title The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii
title_full The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii
title_fullStr The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii
title_full_unstemmed The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii
title_short The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii
title_sort structure of a tautomerase superfamily member linked to the type vi secretion system of acinetobacter baumannii
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9813972/
https://www.ncbi.nlm.nih.gov/pubmed/36598351
http://dx.doi.org/10.1107/S2053230X22011414
work_keys_str_mv AT pankovgenady thestructureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT molavelargabriela thestructureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT buchanangrant thestructureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT coulthurstsarahj thestructureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT hunterwilliamn thestructureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT pankovgenady structureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT molavelargabriela structureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT buchanangrant structureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT coulthurstsarahj structureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii
AT hunterwilliamn structureofatautomerasesuperfamilymemberlinkedtothetypevisecretionsystemofacinetobacterbaumannii