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Biophys J, April 1999, p. 1784-1795, Vol. 76, No. 4
*Orion Corporation,
The structure of a 36-amino-acid-long amino-terminal
fragment of phospholamban (phospholamban[1-36]) in aqueous solution
containing 30% trifluoroethanol was determined by nuclear magnetic
resonance. The peptide, which comprises the cytoplasmic domain and six
residues of the transmembrane domain of phospholamban, assumes a
conformation characterized by two
Biophys J, April 1999, p. 1784-1795, Vol. 76, No. 4
-helices connected by a turn. The
residues of the turn are Ile18, Glu19, Met20, and Pro21, which are
adjacent to the two phosphorylation sites Ser16 and Thr17. The proline is in a trans conformation. The helix comprising amino
acids 22-36 is well determined (the root mean square deviation for the
backbone atoms, calculated for a family of 18 nuclear magnetic
resonance structures is 0.57 Å). Recently, two molecular models of the
transmembrane domain of phospholamban were proposed in which a
symmetric homopentamer is composed of a left-handed coiled coil of
-helices. The two models differ by the relative orientation of the
helices. The model proposed by Simmerman et al. (H.K. Simmerman, Y.M.
Kobayashi, J.M. Autry, and L.R. Jones, 1996, J. Biol. Chem.
271:5941-5946), in which the coiled coil is stabilized by a
leucine-isoleucine zipper, is similar to the transmembrane pentamer
structure of the cartilage oligomeric membrane protein determined
recently by x-ray (V. Malashkevich, R. Kammerer, V. Efimov, T. Schulthess, and J. Engel, 1996, Science 274:761-765). In the model
proposed by Adams et al. (P.D. Adams, I.T. Arkin, D.M. Engelman, and
A.T. Brunger, 1995, Nature Struct. Biol. 2:154-162), the helices in the coiled coil have a different relative orientation, i.e., are rotated clockwise by ~50°. It was possible to overlap and connect the structure of phospholamban[1-36] derived in the present study to
the two transmembrane pentamer models proposed. In this way two models
of the whole phospholamban in its pentameric form were generated. When
our structure was connected to the leucine-isoleucine zipper model, the
inner side of the cytoplasmic domain of the pentamer (where the helices
face one another) was lined by polar residues (Gln23, Gln26, and
Asn30), whereas the five Arg25 side chains were on the outer side. On
the contrary, when our structure was connected to the other
transmembrane model, in the inner side of the cytoplasmic domain of the
pentamer, the five Arg25 residues formed a highly charged cluster.
© 1999 by the Biophysical Society 0006-3495/99/04/1784/12 $2.00
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