1T5E

The structure of MexA

1T5E の概要

• エントリーDOI: 10.2210/pdb1t5e/pdb
• 分子名称: Multidrug resistance protein mexA, GLYCEROL, D-Glyceraldehyde (3 entities in total)
• 機能のキーワード: mexa, antibiotic efflux pump, periplasmic adaptor protein, transport protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 503414.79

構造登録者

Higgins, M.K.,Bokma, E.,Koronakis, E.,Hughes, C.,Koronakis, V. (登録日: 2004-05-04, 公開日: 2004-05-18, 最終更新日: 2024-12-25)

主引用文献

Higgins, M.K.,Bokma, E.,Koronakis, E.,Hughes, C.,Koronakis, V.
Structure of the periplasmic component of a bacterial drug efflux pump
Proc.Natl.Acad.Sci.USA, 101:9994-9999, 2004

PubMed Abstract: Multidrug resistance among Gram-negative bacteria is conferred by three-component membrane pumps that expel diverse antibiotics from the cell. These efflux pumps consist of an inner membrane transporter such as the AcrB proton antiporter, an outer membrane exit duct of the TolC family, and a periplasmic protein known as the adaptor. We present the x-ray structure of the MexA adaptor from the human pathogen Pseudomonas aeruginosa. The elongated molecule contains three linearly arranged subdomains; a 47-A-long alpha-helical hairpin, a lipoyl domain, and a six-stranded beta-barrel. In the crystal, hairpins of neighboring MexA monomers pack side-by-side to form twisted arcs. We discuss the implications of the packing of molecules within the crystal. On the basis of the structure and packing, we suggest a model for the key periplasmic interaction between the outer membrane channel and the adaptor protein in the assembled drug efflux pump.

PubMed: 15226509
DOI: 10.1073/pnas.0400375101

実験手法

X-RAY DIFFRACTION (3 Å)