1JDM

NMR Structure of Sarcolipin

Summary for 1JDM

• Entry DOI: 10.2210/pdb1jdm/pdb
• Descriptor: Sarcolipin (1 entity in total)
• Functional Keywords: helix, membrane protein
• Cellular location: Sarcoplasmic reticulum membrane; Single-pass membrane protein: O00631
• Total number of polymer chains: 1
• Total formula weight: 3763.56

Authors

Veglia, G.,Mascioni, A. (deposition date: 2001-06-14, release date: 2002-02-13, Last modification date: 2024-05-22)

Primary citation

Mascioni, A.,Karim, C.,Barany, G.,Thomas, D.D.,Veglia, G.
Structure and orientation of sarcolipin in lipid environments.
Biochemistry, 41:475-482, 2002

PubMed Abstract: 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.

PubMed: 11781085
DOI: 10.1021/bi011243m

Experimental method

SOLUTION NMR