6BI6
Solution NMR structure of uncharacterized protein YejG
Summary for 6BI6
| Entry DOI | 10.2210/pdb6bi6/pdb |
| NMR Information | BMRB: 30370 |
| Descriptor | Uncharacterized protein YejG (1 entity in total) |
| Functional Keywords | pf13989, yejg, unknown function |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 1 |
| Total formula weight | 12557.15 |
| Authors | Mohanty, B.,Finn, T.J.,Macindoe, I.,Zhong, J.,Patrick, W.M.,Mackay, J.P. (deposition date: 2017-11-01, release date: 2018-11-07, Last modification date: 2024-05-15) |
| Primary citation | Mohanty, B.,Hanson-Manful, P.,Finn, T.J.,Chambers, C.R.,McKellar, J.L.O.,Macindoe, I.,Helder, S.,Setiyaputra, S.,Zhong, Y.,Mackay, J.P.,Patrick, W.M. The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G. Proteins, 87:699-705, 2019 Cited by PubMed Abstract: InterPro family IPR020489 comprises ~1000 uncharacterized bacterial proteins. Previously we showed that overexpressing the Escherichia coli representative of this family, EcYejG, conferred low-level resistance to aminoglycoside antibiotics. In an attempt to shed light on the biochemical function of EcYejG, we have solved its structure using multinuclear solution NMR spectroscopy. The structure most closely resembles that of domain III from elongation factor G (EF-G). EF-G catalyzes ribosomal translocation and mutations in EF-G have also been associated with aminoglycoside resistance. While we were unable to demonstrate a direct interaction between EcYejG and the ribosome, the protein might play a role in translation. PubMed: 30958578DOI: 10.1002/prot.25687 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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