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Abstract <p>ATPase EttA is the most common eubacterial protein of the ABC-F family, which facilitates the conformational transition of the ribosome from one state to another during elongation through a nucleotide-dependent interaction sensitive to the ATP/ADP ratio. Proteins of the ABC-F family confer resistance to antibiotics that bind in the peptidyltransferase center and the ribosomal tunnel; however, the details of the mechanism of action of this protein from <i>Staphylococcus aureus</i> are unclear. A comparison of the amino acid sequences of EttA proteins from <i>S. aureus</i>, <i>Mycobacterium tuberculosis</i>, and <i>Escherichia coli</i> indicates the presence of an additional 75 residues at the C-terminus of the protein, the function of which is unknown. The structure of the <i>Sa</i>EttA protein was analyzed using small-angle X-ray scattering, which revealed a distinct domain arrangement and additional density at the C-terminus of the protein.</p>

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Structural Studies of the ATP-Binding Protein EttA from the Pathogenic Bacterium Staphylococcus aureus by Small-angle X-ray Scattering

  • 期刊论文

  • 发表日期：

    2025年12月26日

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  • A. E. Gimaletdinova,
  • E. S. Kuchaev,
  • V. E. Gonialin,
  • P. V. Egorova,
  • S. A. Ryabov,
  • M. S. Glazyrin,
  • N. A. Smolyanova,
  • N. S. Garaeva,
  • D. D. Kuklina,
  • Yu. L. Ryzhykau,
  • M. M. Yusupov,
  • K. S. Usachev

摘要

Abstract

ATPase EttA is the most common eubacterial protein of the ABC-F family, which facilitates the conformational transition of the ribosome from one state to another during elongation through a nucleotide-dependent interaction sensitive to the ATP/ADP ratio. Proteins of the ABC-F family confer resistance to antibiotics that bind in the peptidyltransferase center and the ribosomal tunnel; however, the details of the mechanism of action of this protein from Staphylococcus aureus are unclear. A comparison of the amino acid sequences of EttA proteins from S. aureus, Mycobacterium tuberculosis, and Escherichia coli indicates the presence of an additional 75 residues at the C-terminus of the protein, the function of which is unknown. The structure of the SaEttA protein was analyzed using small-angle X-ray scattering, which revealed a distinct domain arrangement and additional density at the C-terminus of the protein.