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The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G
Author(s) -
Mohanty Biswaranjan,
HansonManful Paulina,
Finn Thomas J.,
Chambers Cecilia R.,
McKellar James L. O.,
Macindoe Ingrid,
Helder Stephanie,
Setiyaputra Surya,
Zhong Yichen,
Mackay Joel P.,
Patrick Wayne M.
Publication year - 2019
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25687
Subject(s) - ribosome , elongation factor , escherichia coli , ribosomal protein , translation (biology) , ribosomal rna , chemistry , protein biosynthesis , biology , biochemistry , rna , gene , messenger rna
InterPro family IPR020489 comprises ~1000 uncharacterized bacterial proteins. Previously we showed that overexpressing the Escherichia coli representative of this family, Ec YejG, conferred low‐level resistance to aminoglycoside antibiotics. In an attempt to shed light on the biochemical function of Ec YejG, 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 Ec YejG and the ribosome, the protein might play a role in translation.