3B5D

EmrE multidrug transporter in complex with TPP, C2 crystal form

3B5D の概要

• エントリーDOI: 10.2210/pdb3b5d/pdb
• 分子名称: Multidrug transporter emrE, TETRAPHENYLPHOSPHONIUM (2 entities in total)
• 機能のキーワード: helical membrane protein, multidrug resistance transporter, smr, antiport, inner membrane, transmembrane, joint center for innovative membrane protein technologies, membrane protein
• 由来する生物種: Escherichia coli K12
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P23895
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24265.94

構造登録者

Chang, G.,Chen, Y.J. (登録日: 2007-10-25, 公開日: 2007-12-04, 最終更新日: 2024-02-21)

主引用文献

Chen, Y.J.,Pornillos, O.,Lieu, S.,Ma, C.,Chen, A.P.,Chang, G.
X-ray structure of EmrE supports dual topology model.
Proc.Natl.Acad.Sci.Usa, 104:18999-19004, 2007

PubMed Abstract: EmrE, a multidrug transporter from Escherichia coli, functions as a homodimer of a small four-transmembrane protein. The membrane insertion topology of the two monomers is controversial. Although the EmrE protein was reported to have a unique orientation in the membrane, models based on electron microscopy and now defunct x-ray structures, as well as recent biochemical studies, posit an antiparallel dimer. We have now reanalyzed our x-ray data on EmrE. The corrected structures in complex with a transport substrate are highly similar to the electron microscopy structure. The first three transmembrane helices from each monomer surround the substrate binding chamber, whereas the fourth helices participate only in dimer formation. Selenomethionine markers clearly indicate an antiparallel orientation for the monomers, supporting a "dual topology" model.

PubMed: 18024586
DOI: 10.1073/pnas.0709387104

実験手法

X-RAY DIFFRACTION (3.8 Å)