1jdm

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdm OCA], [http://www.ebi.ac.uk/pdbsum/1jdm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdm RCSB]</span>
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Revision as of 18:32, 30 March 2008


PDB ID 1jdm

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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