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The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G.
Mohanty, Biswaranjan; Hanson-Manful, 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.
Afiliação
  • Mohanty B; Faculty of Pharmacy and Pharmaceutical Sciences, Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Australia.
  • Hanson-Manful P; Institute of Natural and Mathematical Sciences, Massey University, Auckland, New Zealand.
  • Finn TJ; Department of Biochemistry, University of Otago, Dunedin, New Zealand.
  • Chambers CR; Department of Biochemistry, University of Otago, Dunedin, New Zealand.
  • McKellar JLO; Department of Biochemistry, University of Otago, Dunedin, New Zealand.
  • Macindoe I; School of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Helder S; School of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Setiyaputra S; School of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Zhong Y; School of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Mackay JP; School of Life and Environmental Sciences, The University of Sydney, Sydney, New South Wales, Australia.
  • Patrick WM; School of Biological Sciences, Victoria University, Wellington, New Zealand.
Proteins ; 87(8): 699-705, 2019 08.
Article em En | MEDLINE | ID: mdl-30958578
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fator G para Elongação de Peptídeos / Proteínas de Escherichia coli / Escherichia coli Tipo de estudo: Prognostic_studies Idioma: En Revista: Proteins Assunto da revista: BIOQUIMICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Austrália

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fator G para Elongação de Peptídeos / Proteínas de Escherichia coli / Escherichia coli Tipo de estudo: Prognostic_studies Idioma: En Revista: Proteins Assunto da revista: BIOQUIMICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Austrália