7YXV
Crystal structure of a tautomerase superfamily member form Acinetobacter baumanii
Summary for 7YXV
Entry DOI | 10.2210/pdb7yxv/pdb |
Descriptor | Anthranilate synthase, NITRATE ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | cytosolic protein, tautomerase superfamily, 4-oxalocrotonate tautomerase, t6ss |
Biological source | Acinetobacter baumannii |
Total number of polymer chains | 1 |
Total formula weight | 15413.08 |
Authors | Pankov, G.,Hunter, W.N. (deposition date: 2022-02-16, release date: 2022-05-18, Last modification date: 2024-02-07) |
Primary citation | Pankov, 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: 36598351DOI: 10.1107/S2053230X22011414 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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