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New page: left|200px<br /> <applet load="1jdm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdm" /> '''NMR Structure of Sarcolipin'''<br /> ==Ove...
 
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[[Image:1jdm.gif|left|200px]]<br />
<applet load="1jdm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jdm" />
'''NMR Structure of Sarcolipin'''<br />


==Overview==
==NMR Structure of Sarcolipin==
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.
<StructureSection load='1jdm' size='340' side='right'caption='[[1jdm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jdm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdm OCA], [https://pdbe.org/1jdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdm RCSB], [https://www.ebi.ac.uk/pdbsum/1jdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SARCO_HUMAN SARCO_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:11781085</ref>
1JDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JDM OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11781085 11781085]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1jdm" style="background-color:#fffaf0;"></div>
[[Category: Mascioni, A.]]
== References ==
[[Category: Veglia, G.]]
<references/>
[[Category: helix]]
__TOC__
 
</StructureSection>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:39:44 2007''
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mascioni A]]
[[Category: Veglia G]]

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NMR Structure of Sarcolipin

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