4TKO

Structure of the periplasmic adaptor protein EmrA

4TKO の概要

• エントリーDOI: 10.2210/pdb4tko/pdb
• 分子名称: EmrA, MAGNESIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: mfs, multidrug resistance, periplasmic adaptor, membrane protein
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41466.82

構造登録者

Hinchliffe, P.,Greene, N.P.,Paterson, N.G.,Crow, A.,Hughes, C.,Koronakis, V. (登録日: 2014-05-27, 公開日: 2014-07-09, 最終更新日: 2023-12-27)

主引用文献

Hinchliffe, P.,Greene, N.P.,Paterson, N.G.,Crow, A.,Hughes, C.,Koronakis, V.
Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump.
Febs Lett., 588:3147-3153, 2014

PubMed Abstract: Periplasmic adaptor proteins are key components of bacterial tripartite efflux pumps. The 2.85 Å resolution structure of an MFS (major facilitator superfamily) pump adaptor, Aquifex aeolicus EmrA, shows linearly arranged α-helical coiled-coil, lipoyl, and β-barrel domains, but lacks the fourth membrane-proximal domain shown in other pumps to interact with the inner membrane transporter. The adaptor α-hairpin, which binds outer membrane TolC, is exceptionally long at 127 Å, and the β-barrel contains a conserved disordered loop. The structure extends the view of adaptors as flexible, modular components that mediate diverse pump assembly, and suggests that in MFS tripartite pumps a hexamer of adaptors could provide a periplasmic seal.

PubMed: 24996185
DOI: 10.1016/j.febslet.2014.06.055

実験手法

X-RAY DIFFRACTION (2.85 Å)