4nab: Difference between revisions
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The | ==Structure of the (SR)Ca2+-ATPase mutant E309Q in the Ca2-E1-MgAMPPCP form== | ||
<StructureSection load='4nab' size='340' side='right'caption='[[4nab]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4nab]] 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=4NAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NAB 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]] 3.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</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=4nab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nab OCA], [https://pdbe.org/4nab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nab RCSB], [https://www.ebi.ac.uk/pdbsum/4nab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nab ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) couples ATP hydrolysis to transport of Ca(2+). This directed energy transfer requires cross-talk between the two Ca(2+) sites and the phosphorylation site over 50 A distance. We have addressed the mechano-structural basis for this intramolecular signal by analysing the structure and the functional properties of SERCA mutant E309Q. Glu(309) contributes to Ca(2+) coordination at site II, and a consensus has been that E309Q only binds Ca(2+) at site I. The crystal structure of E309Q in the presence of Ca(2+) and an ATP analogue, however, reveals two occupied Ca(2+) sites of a non-catalytic Ca2E1 state. Ca(2+) is bound with micromolar affinity by both Ca(2+) sites in E309Q, but without cooperativity. The Ca(2+)-bound mutant does phosphorylate from ATP, but at a very low maximal rate. Phosphorylation depends on the correct positioning of the A-domain, requiring a shift of transmembrane segment M1 into an 'up and kinked position'. This transition is impaired in the E309Q mutant, most likely due to a lack of charge neutralization and altered hydrogen binding capacities at Ca(2+) site II. | |||
SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically incompetent conformation.,Clausen JD, Bublitz M, Arnou B, Montigny C, Jaxel C, Moller JV, Nissen P, Andersen JP, le Maire M EMBO J. 2013 Dec 11;32(24):3231-43. doi: 10.1038/emboj.2013.250. Epub 2013 Nov, 22. PMID:24270570<ref>PMID:24270570</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4nab" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: Andersen JP]] | |||
[[Category: Arnou B]] | |||
[[Category: Bublitz M]] | |||
[[Category: Clausen JD]] | |||
[[Category: Jaxel C]] | |||
[[Category: Moller JV]] | |||
[[Category: Montigny C]] | |||
[[Category: Nissen P]] | |||
[[Category: Le Maire M]] | |||
