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Published online before print September 28, 2007, 10.1110/ps.072977707
Protein Science (2007), 16:2345-2349. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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ACCELERATED COMMUNICATION

The structural topology of wild-type phospholamban in oriented lipid bilayers using 15N solid-state NMR spectroscopy

Shadi Abu-Baker1,3, Jun-Xia Lu1,3, Shidong Chu1, Kiran K. Shetty2, Peter L. Gor'kov2, and Gary A. Lorigan1

1 Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, USA
2 National High Magnetic Field Laboratory, Tallahassee, Florida 32310, USA

(RECEIVED April 30, 2007; FINAL REVISION August 23, 2007; ACCEPTED August 23, 2007)

For the first time, 15N solid-state NMR experiments were conducted on wild-type phospholamban (WT-PLB) embedded inside mechanically oriented phospholipid bilayers to investigate the topology of its cytoplasmic and transmembrane domains. 15N solid-state NMR spectra of site-specific 15N-labeled WT-PLB indicate that the transmembrane domain has a tilt angle of 13° ± 6° with respect to the POPC (1-palmitoyl-2-oleoyl-sn-glycero-phosphocholine) bilayer normal and that the cytoplasmic domain of WT-PLB lies on the surface of the phospholipid bilayers. Comparable results were obtained from site-specific 15N-labeled WT-PLB embedded inside DOPC/DOPE (1,2-dioleoyl-sn-glycero-3-phosphocholine/1,2-dioleoyl-sn-glycero-3-phosphoethanolamine) mechanically oriented phospholipids' bilayers. The new NMR data support a pinwheel geometry of WT-PLB, but disagree with a bellflower structure in micelles, and indicate that the orientation of the cytoplasmic domain of the WT-PLB is similar to that reported for the monomeric AFA-PLB mutant.

Keywords: wild-type phospholamban; oriented phospholipids; structural topology; 15N solid-state NMR spectroscopy


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