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J. Biol. Chem., Vol. 277, Issue 42, 40125-40131, October 18, 2002

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Projection Structure of P-glycoprotein by Electron Microscopy
EVIDENCE FOR A CLOSED CONFORMATION OF THE NUCLEOTIDE BINDING DOMAINS^*

Jyh-Yeuan Lee, Ina L. Urbatsch^§, Alan E. Senior^§, and Stephan Wilkens^¶

From the  University of California, Riverside, Department of Biochemistry, Riverside, California 92521 and the ^§ University of Rochester Medical Center, Department of Biochemistry and Biophysics, Rochester, New York 14642

The structure of P-glycoprotein (Pgp) from mouse has been studied by electron microscopy and image analysis. Two-dimensional crystals of Pgp in a lipid bilayer were generated by reconstituting pure, detergent-solubilized protein containing a C-terminal six-histidine tag using the lipid monolayer technique. The crystals belong to plane group P1 with a = b = 104 ± 2 Å and  = 90 ± 4°. The projection structure of Pgp calculated at a resolution of 22 Å shows two closely interacting protein domains that can be interpreted as the N- and C-terminal halves of the protein. The projection structure of Pgp is consistent with the recently published x-ray structure of MsbA, a lipid A flippase from Escherichia coli with high sequence homology to Pgp but only when the two MsbA subunits are rotated to bring their nucleotide binding domains together.

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