1PJD

Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers

Summary for 1PJD

• Entry DOI: 10.2210/pdb1pjd/pdb
• Descriptor: Pheromone alpha factor receptor (1 entity in total)
• Functional Keywords: alpha helix, membrane protein
• Cellular location: Membrane; Multi-pass membrane protein: P06842
• Total number of polymer chains: 1
• Total formula weight: 1977.41

Authors

Valentine, K.G.,Liu, S.-F.,Marassi, F.M.,Veglia, G.,Nevzorov, A.A.,Opella, S.J.,Ding, F.-X.,Wang, S.-H.,Arshava, B.,Becker, J.M.,Naider, F. (deposition date: 2003-06-02, release date: 2003-09-16, Last modification date: 2024-05-22)

Primary citation

Valentine, K.G.,Liu, S.-F.,Marassi, F.M.,Veglia, G.,Opella, S.J.,Ding, F.-X.,Wang, S.-H.,Arshava, B.,Becker, J.M.,Naider, F.
Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers
Biopolymers, 59:243-256, 2001

PubMed Abstract: A detailed analysis of the structure of an 18-residue peptide AQSLLVPSIIFILAYSLK [M6(252-269, C252A)] in 1,2-dimyristoyl-sn-glycero-phosphocholine bilayers was carried out using solid state NMR and attenuated total reflection Fourier transform infrared spectroscopy. The peptide corresponds to a portion of the 6th transmembrane domain of the alpha-factor receptor of Saccharomyces cerevisiae. Ten homologs of M6(252-269, C252A) were synthesized in which individual residues were labeled with (15)N. One- and two-dimensional solid state NMR experiments were used to determine the chemical shifts and (1)H-(15)N dipolar coupling constants for the (15)N-labeled peptides in oriented dimyristoylphosphatidylcholine bilayers on stacked glass plates. These parameters were used to calculate the structure and orientation of M6(252-269, C252A) in the bilayers. The results indicate that the carboxyl terminal residues (9-14) are alpha-helical and oriented with an angle of about 8 degrees with respect to the bilayer normal. Independently, an attenuated total reflection Fourier transform infrared spectroscopy analysis on M6(252-269, C252A) in a 1,2-dimyristoyl-sn-glycero-phosphocholine bilayer concluded that the helix tilt angle was about 12.5 degrees. The results on the structure of M6(252-269, C252A) in bilayers are in good agreement with the structure determined in trifluoroethanol/water solutions (B. Arshava et al. Biopolymers, 1998, Vol. 46, pp. 343-357). The present study shows that solid state NMR spectroscopy can provide high resolution information on the structure of transmembrane domains of a G protein-coupled receptor.

PubMed: 11473349
DOI: 10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H

Experimental method

SOLID-STATE NMR