Structure of a bacterial multidrug ABC transporter

Article Abstract:

The 3.0-angstrom crystal structure of a bacterial ATP transporter (Sav1866) from Staphylococcus aureus is determined to study the molecular process of the multidrug transporters of the ABC family. The homodimeric protein consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1, but critically different from that reported for the bacterial lipid flippase MsbA.

Staphylococcus aureus, Adenosine triphosphatase, ATPases

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Crystal structure of a rhomboid family intramembrane protease

Article Abstract:

The crystal structure of the Escherichia coli GlpG core domain is described. The analysis has indicated that, in intramembrane proteolysis, the scission of peptide bonds takes place within the hydrophobic environment of the membrane bilayer and the crystal structure has suggested a gating mechanism for GlpG that controls substrate access to its hydrophilic active site.

Observations, Escherichia coli, Proteolysis, Hydrophobic effect

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Structure of an ABC transporter in complex with its binding protein

Article Abstract:

Mechanism of ATP-binding cassette (ABC) transporter proteins is studied with help of molybdate transporter from Archaeoglobus fulgidus in complex with its binding protein. It is revealed that binding of ATP promotes an outward facing conformation.

United States, Carrier proteins, Transport proteins, Cancer, Cancer genetics, Structure, Chemical properties, Adenosine triphosphatase genes, ATP genes, Report

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