3w5c: Difference between revisions
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==Crystal structure of the calcium pump in the E2 state free from exogenous inhibitors== | ==Crystal structure of the calcium pump in the E2 state free from exogenous inhibitors== | ||
<StructureSection load='3w5c' size='340' side='right' caption='[[3w5c]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3w5c' size='340' side='right'caption='[[3w5c]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3w5c]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3w5c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W5C FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></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=3w5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w5c OCA], [https://pdbe.org/3w5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w5c RCSB], [https://www.ebi.ac.uk/pdbsum/3w5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w5c ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3w5c" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ATPase|ATPase]] | *[[ATPase 3D structures|ATPase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Hirata | [[Category: Hirata A]] | ||
[[Category: Inesi | [[Category: Inesi G]] | ||
[[Category: Iwasawa | [[Category: Iwasawa S]] | ||
[[Category: Ogawa | [[Category: Ogawa H]] | ||
[[Category: Toyoshima | [[Category: Toyoshima C]] | ||
[[Category: Tsueda | [[Category: Tsueda J]] | ||
Latest revision as of 05:35, 21 November 2024
Crystal structure of the calcium pump in the E2 state free from exogenous inhibitorsCrystal structure of the calcium pump in the E2 state free from exogenous inhibitors
Structural highlights
Publication Abstract from PubMedP-type ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes, and are distinct from other ATPases in that the reaction cycle includes an autophosphorylation step. The best studied is Ca(2+)-ATPase from muscle sarcoplasmic reticulum (SERCA1a), a Ca(2+) pump that relaxes muscle cells after contraction, and crystal structures have been determined for most of the reaction intermediates. An important outstanding structure is that of the E1 intermediate, which has empty high-affinity Ca(2+)-binding sites ready to accept new cytosolic Ca(2+). In the absence of Ca(2+) and at pH 7 or higher, the ATPase is predominantly in E1, not in E2 (low affinity for Ca(2+)), and if millimolar Mg(2+) is present, one Mg(2+) is expected to occupy one of the Ca(2+)-binding sites with a millimolar dissociation constant. This Mg(2+) accelerates the reaction cycle, not permitting phosphorylation without Ca(2+) binding. Here we describe the crystal structure of native SERCA1a (from rabbit) in this E1.Mg(2+) state at 3.0 A resolution in addition to crystal structures of SERCA1a in E2 free from exogenous inhibitors, and address the structural basis of the activation signal for phosphoryl transfer. Unexpectedly, sarcolipin, a small regulatory membrane protein of Ca(2+)-ATPase, is bound, stabilizing the E1.Mg(2+) state. Sarcolipin is a close homologue of phospholamban, which is a critical mediator of beta-adrenergic signal in Ca(2+) regulation in heart (for reviews, see, for example, refs 8-10), and seems to play an important role in muscle-based thermogenesis. We also determined the crystal structure of recombinant SERCA1a devoid of sarcolipin, and describe the structural basis of inhibition by sarcolipin/phospholamban. Thus, the crystal structures reported here fill a gap in the structural elucidation of the reaction cycle and provide a solid basis for understanding the physiological regulation of the calcium pump. Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state.,Toyoshima C, Iwasawa S, Ogawa H, Hirata A, Tsueda J, Inesi G Nature. 2013 Mar 14;495(7440):260-4. doi: 10.1038/nature11899. Epub 2013 Mar 3. PMID:23455422[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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