1jdm
From Proteopedia
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NMR Structure of Sarcolipin
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.
About this Structure
1JDM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure and orientation of sarcolipin in lipid environments., Mascioni A, Karim C, Barany G, Thomas DD, Veglia G, Biochemistry. 2002 Jan 15;41(2):475-82. PMID:11781085
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