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{{STRUCTURE_3n8g|  PDB=3n8g  |  SCENE=  }}
===Structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form===
{{ABSTRACT_PUBMED_23400778}}


==About this Structure==
==Structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form==
[[3n8g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N8G OCA].  
<StructureSection load='3n8g' size='340' side='right'caption='[[3n8g]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3n8g]] 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=3N8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N8G FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.585&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=3n8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n8g OCA], [https://pdbe.org/3n8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n8g RCSB], [https://www.ebi.ac.uk/pdbsum/3n8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n8g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The sarco(endo)plasmic reticulum Ca2+- ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPases. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco-endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This article focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion binding sites of SERCA are accessible from either the cytoplasm or the SR/ER lumen at a time, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane (TM) alpha-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the Cterminal TM region leading from the ion binding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+- free E2-states, suggesting that it may play a functional role in proton release from the ion binding sites. This is in agreement with molecular dynamics (MD) simulations, mutational studies, and in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not only one, but two cytoplasmic pathways working in concert.
 
Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.,Bublitz M, Musgaard M, Poulsen H, Thogersen L, Olesen C, Schiott B, Morth JP, Moller JV, Nissen P J Biol Chem. 2013 Feb 11. PMID:23400778<ref>PMID:23400778</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3n8g" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:023400778</ref><references group="xtra"/><references/>
__TOC__
[[Category: Calcium-transporting ATPase]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Bublitz, M.]]
[[Category: Bublitz M]]
[[Category: Moller, J V.]]
[[Category: Moller JV]]
[[Category: Morth, J P.]]
[[Category: Morth JP]]
[[Category: Nissen, P.]]
[[Category: Nissen P]]
[[Category: Olesen, C.]]
[[Category: Olesen C]]
[[Category: Poulsen, H.]]
[[Category: Poulsen H]]
[[Category: Adenosine diphosphate]]
[[Category: Adenosine triphosphate]]
[[Category: Aluminum compound]]
[[Category: Calcium-transporting atpase]]
[[Category: Crystallization]]
[[Category: Cytosol]]
[[Category: Fast-twitch]]
[[Category: Fluoride]]
[[Category: Hydrolase]]
[[Category: Muscle fiber]]
[[Category: Phosphorylation]]
[[Category: Protein conformation]]
[[Category: Sarcoplasmic reticulum calcium-transporting atpase]]

Latest revision as of 09:10, 6 September 2023

Structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form

3n8g, resolution 2.58Å

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