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J. Biol. Chem., Vol. 277, Issue 42, 40125-40131, October 18, 2002
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From the 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
Projection Structure of P-glycoprotein by Electron Microscopy
EVIDENCE FOR A CLOSED CONFORMATION OF THE NUCLEOTIDE BINDING
DOMAINS*
,¶
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
= 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.
*
This work was supported by National Institutes of Health
Grants GM58600 (to S. W.) and GM50156 (to A. E. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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