1jdm: Difference between revisions

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==Overview==

Sarcolipin (SLN) is a 31 amino acid integral membrane protein that, regulates Ca-ATPase activity in skeletal muscle. Here, we report the, three-dimensional structure and topology of synthetic SLN in lipid, environments, as determined by solution and solid-state NMR spectroscopy., 2D solution NMR experiments were performed on SLN solubilized in sodium, dodecyl sulfate (SDS) micelles. We found that SLN adopts a highly defined, alpha-helical conformation from F9 through R27, with a backbone RMSD of, 0.65 A and a side chain RMSD of 1.66 A. The N-terminus (M1 through L8) and, the C-terminus (S28 through Y31) are mostly unstructured. The orientation, of the SLN was determined using one-dimensional (15)N NMR solid-state, spectroscopy. The protein was incorporated into phospholipid bilayers, prepared from a mixture of 1,2-dioleoyl-sn-glycero-3-phosphocholine and, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine. The (15)N chemical shift, solid-state spectra from selectively labeled SLN samples indicate that SLN, orients perpendicularly to the plane of the membrane bilayers. These, results support the proposed mechanism of Ca-ATPase regulation of SLN via, protein-protein intramembranous interactions between the highly conserved, transmembrane domains of the Ca-ATPase and the conserved transmembrane, domain of SLN.

Sarcolipin (SLN) is a 31 amino acid integral membrane protein that regulates Ca-ATPase activity in skeletal muscle. Here, we report the three-dimensional structure and topology of synthetic SLN in lipid environments, as determined by solution and solid-state NMR spectroscopy. 2D solution NMR experiments were performed on SLN solubilized in sodium dodecyl sulfate (SDS) micelles. We found that SLN adopts a highly defined alpha-helical conformation from F9 through R27, with a backbone RMSD of 0.65 A and a side chain RMSD of 1.66 A. The N-terminus (M1 through L8) and the C-terminus (S28 through Y31) are mostly unstructured. The orientation of the SLN was determined using one-dimensional (15)N NMR solid-state spectroscopy. The protein was incorporated into phospholipid bilayers prepared from a mixture of 1,2-dioleoyl-sn-glycero-3-phosphocholine and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine. The (15)N chemical shift solid-state spectra from selectively labeled SLN samples indicate that SLN orients perpendicularly to the plane of the membrane bilayers. These results support the proposed mechanism of Ca-ATPase regulation of SLN via protein-protein intramembranous interactions between the highly conserved transmembrane domains of the Ca-ATPase and the conserved transmembrane domain of SLN.

==About this Structure==

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[[Category: helix]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:26 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Sarcolipin (SLN) is a 31 amino acid integral membrane protein that, regulates Ca-ATPase activity in skeletal muscle. Here, we report the, three-dimensional structure and topology of synthetic SLN in lipid, environments, as determined by solution and solid-state NMR spectroscopy., 2D solution NMR experiments were performed on SLN solubilized in sodium, dodecyl sulfate (SDS) micelles. We found that SLN adopts a highly defined, alpha-helical conformation from F9 through R27, with a backbone RMSD of, 0.65 A and a side chain RMSD of 1.66 A. The N-terminus (M1 through L8) and, the C-terminus (S28 through Y31) are mostly unstructured. The orientation, of the SLN was determined using one-dimensional (15)N NMR solid-state, spectroscopy. The protein was incorporated into phospholipid bilayers, prepared from a mixture of 1,2-dioleoyl-sn-glycero-3-phosphocholine and, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine. The (15)N chemical shift, solid-state spectra from selectively labeled SLN samples indicate that SLN, orients perpendicularly to the plane of the membrane bilayers. These, results support the proposed mechanism of Ca-ATPase regulation of SLN via, protein-protein intramembranous interactions between the highly conserved, transmembrane domains of the Ca-ATPase and the conserved transmembrane, domain of SLN.
+Sarcolipin (SLN) is a 31 amino acid integral membrane protein that regulates Ca-ATPase activity in skeletal muscle. Here, we report the three-dimensional structure and topology of synthetic SLN in lipid environments, as determined by solution and solid-state NMR spectroscopy. 2D solution NMR experiments were performed on SLN solubilized in sodium dodecyl sulfate (SDS) micelles. We found that SLN adopts a highly defined alpha-helical conformation from F9 through R27, with a backbone RMSD of 0.65 A and a side chain RMSD of 1.66 A. The N-terminus (M1 through L8) and the C-terminus (S28 through Y31) are mostly unstructured. The orientation of the SLN was determined using one-dimensional (15)N NMR solid-state spectroscopy. The protein was incorporated into phospholipid bilayers prepared from a mixture of 1,2-dioleoyl-sn-glycero-3-phosphocholine and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine. The (15)N chemical shift solid-state spectra from selectively labeled SLN samples indicate that SLN orients perpendicularly to the plane of the membrane bilayers. These results support the proposed mechanism of Ca-ATPase regulation of SLN via protein-protein intramembranous interactions between the highly conserved transmembrane domains of the Ca-ATPase and the conserved transmembrane domain of SLN.
 ==About this Structure==
@@ Line 16: / Line 16: @@
 [[Category: helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:06:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:26 2008''