期刊
SCIENCE
卷 312, 期 5774, 页码 741-744出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1125629
关键词
-
资金
- NIGMS NIH HHS [R21 GM065798-01, GM70480, R01 GM070480, GM65798, R21 GM065798-02] Funding Source: Medline
EmrD is a multidrug transporter from the Major Facilitator Superfamily that expels amphipathic compounds across the inner membrane of Escherichia coli. Here, we report the x-ray structure of EmrD determined to a resolution of 3.5 angstroms. The structure reveals an interior that is composed mostly of hydrophobic residues, which is consistent with its role transporting amphipathic molecules. Two long loops extend into the inner leaflet side of the cell membrane. This region can serve to recognize and bind substrate directly from the lipid bilayer. We propose that multisubstrate specificity, binding, and transport are facilitated by these loop regions and the internal cavity.
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