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==Calcium ATPase-1 from Listeria monocytogenes in complex with BeF==
<StructureSection load='6zhf' size='340' side='right'caption='[[6zhf]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZHF 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]] 4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6zhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zhf OCA], [https://pdbe.org/6zhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zhf RCSB], [https://www.ebi.ac.uk/pdbsum/6zhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zhf ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA). Here we present three crystal structures of Ca(2+)-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF3(-) mimicking a phosphoenzyme state reveal a closed state, which is intermediate between the outward-open E2P and the proton-occluded E2-P* conformations known for SERCA. It suggests that LMCA1 in the E2P state is pre-organized for dephosphorylation upon Ca(2+) release, consistent with the rapid dephosphorylation observed in single-molecule studies. An arginine side-chain occupies the position equivalent to calcium binding site I in SERCA, leaving a single Ca(2+)-binding site in LMCA1, corresponding to SERCA site II. Observing no putative transport pathways dedicated to protons, we infer a direct proton counter transport through the Ca(2+) exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.

The crystal structure of the Ca(2+)-ATPase 1 from Listeria monocytogenes reveals a pump primed for dephosphorylation.,Basse Hansen S, Dyla M, Neumann C, Meldgaard Hoegh Quistgaard E, Lauwring Andersen J, Kjaergaard M, Nissen P J Mol Biol. 2021 Apr 29:167015. doi: 10.1016/j.jmb.2021.167015. PMID:33933469<ref>PMID:33933469</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6zhf" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Basse Hansen S]]
[[Category: Dyla M]]
[[Category: Kjaergaard M]]
[[Category: Lauwring Andersen J]]
[[Category: Neumann C]]
[[Category: Nissen P]]
[[Category: Quistgaard EMH]]