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7YXV

Crystal structure of a tautomerase superfamily member form Acinetobacter baumanii

Summary for 7YXV
Entry DOI10.2210/pdb7yxv/pdb
DescriptorAnthranilate synthase, NITRATE ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordscytosolic protein, tautomerase superfamily, 4-oxalocrotonate tautomerase, t6ss
Biological sourceAcinetobacter baumannii
Total number of polymer chains1
Total formula weight15413.08
Authors
Pankov, G.,Hunter, W.N. (deposition date: 2022-02-16, release date: 2022-05-18, Last modification date: 2024-02-07)
Primary citationPankov, G.,Mol Avelar, G.,Buchanan, G.,Coulthurst, S.J.,Hunter, W.N.
The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii.
Acta Crystallogr.,Sect.F, 79:8-16, 2023
Cited by
PubMed 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.
PubMed: 36598351
DOI: 10.1107/S2053230X22011414
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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