6BI6

Solution NMR structure of uncharacterized protein YejG

6BI6 の概要

• エントリーDOI: 10.2210/pdb6bi6/pdb
• NMR情報: BMRB: 30370
• 分子名称: Uncharacterized protein YejG (1 entity in total)
• 機能のキーワード: pf13989, yejg, unknown function
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12557.15

構造登録者

Mohanty, B.,Finn, T.J.,Macindoe, I.,Zhong, J.,Patrick, W.M.,Mackay, J.P. (登録日: 2017-11-01, 公開日: 2018-11-07, 最終更新日: 2024-05-15)

主引用文献

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

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: 30958578
DOI: 10.1002/prot.25687

実験手法

SOLUTION NMR