Structural highlights
Function
A0A077GKT8_ACIBA
Publication Abstract from PubMed
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 beta-alpha-beta 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.
The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii.,Pankov G, Mol Avelar G, Buchanan G, Coulthurst SJ, Hunter WN Acta Crystallogr F Struct Biol Commun. 2023 Jan 1;79(Pt 1):8-16. doi: , 10.1107/S2053230X22011414. Epub 2023 Jan 1. PMID:36598351[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pankov G, Mol Avelar G, Buchanan G, Coulthurst SJ, Hunter WN. The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii. Acta Crystallogr F Struct Biol Commun. 2023 Jan 1;79(Pt 1):8-16. doi: , 10.1107/S2053230X22011414. Epub 2023 Jan 1. PMID:36598351 doi:http://dx.doi.org/10.1107/S2053230X22011414
