6zhh: Difference between revisions
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==Ca2+-ATPase from Listeria Monocytogenes with G4 insertion.== | ==Ca2+-ATPase from Listeria Monocytogenes with G4 insertion.== | ||
<StructureSection load='6zhh' size='340' side='right'caption='[[6zhh]]' scene=''> | <StructureSection load='6zhh' size='340' side='right'caption='[[6zhh]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZHH FirstGlance]. <br> | <table><tr><td colspan='2'>[[6zhh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZHH FirstGlance]. <br> | ||
</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=6zhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zhh OCA], [https://pdbe.org/6zhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zhh RCSB], [https://www.ebi.ac.uk/pdbsum/6zhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zhh ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6zhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zhh OCA], [https://pdbe.org/6zhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zhh RCSB], [https://www.ebi.ac.uk/pdbsum/6zhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zhh ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/LMCA1_LISMO LMCA1_LISMO] Catalyzes the hydrolysis of ATP coupled with the transport of calcium. The transport is electrogenic with a probable ATP:Ca(2+):H(+) stoichiometry of 1:1:1. May have an important role in survival of the bacterium when stressed by a combination of a high calcium concentration and alkaline pH.<ref>PMID:21047776</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6zhh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Listeria monocytogenes]] | |||
[[Category: Basse Hansen S]] | [[Category: Basse Hansen S]] | ||
[[Category: Dyla M]] | [[Category: Dyla M]] | ||
Latest revision as of 16:49, 24 January 2024
Ca2+-ATPase from Listeria Monocytogenes with G4 insertion.Ca2+-ATPase from Listeria Monocytogenes with G4 insertion.
Structural highlights
FunctionLMCA1_LISMO Catalyzes the hydrolysis of ATP coupled with the transport of calcium. The transport is electrogenic with a probable ATP:Ca(2+):H(+) stoichiometry of 1:1:1. May have an important role in survival of the bacterium when stressed by a combination of a high calcium concentration and alkaline pH.[1] Publication Abstract from PubMedMany 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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