6a69: Difference between revisions
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==Cryo-EM structure of a P-type ATPase== | |||
<StructureSection load='6a69' size='340' side='right' caption='[[6a69]], [[Resolution|resolution]] 4.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a69]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A69 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a69 OCA], [http://pdbe.org/6a69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a69 RCSB], [http://www.ebi.ac.uk/pdbsum/6a69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a69 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/AT2B1_HUMAN AT2B1_HUMAN]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. [[http://www.uniprot.org/uniprot/NPTN_HUMAN NPTN_HUMAN]] Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plasma membrane Ca(2+)-ATPases (PMCAs) are key regulators of global Ca(2+) homeostasis and local intracellular Ca(2+) dynamics. Recently, Neuroplastin (NPTN) and basigin were identified as previously unrecognized obligatory subunits of PMCAs that dramatically increase the efficiency of PMCA-mediated Ca(2+) clearance. Here, we report the cryo-EM structure of human PMCA1 (hPMCA1) in complex with NPTN at a resolution of 4.1 A for the overall structure and 3.9 A for the transmembrane domain. The single transmembrane helix of NPTN interacts with the TM8-9-linker and TM10 of hPMCA1. The subunits are required for the hPMCA1 functional activity. The NPTN-bound hPMCA1 closely resembles the E1-Mg(2+) structure of endo(sarco)plasmic reticulum Ca(2+) ATPase and the Ca(2+) site is exposed through a large open cytoplasmic pathway. This structure provides insight into how the subunits bind to the PMCAs and serves as an important basis for understanding the functional mechanisms of this essential calcium pump family. | |||
Structure of the human plasma membrane Ca(2+)-ATPase 1 in complex with its obligatory subunit neuroplastin.,Gong D, Chi X, Ren K, Huang G, Zhou G, Yan N, Lei J, Zhou Q Nat Commun. 2018 Sep 6;9(1):3623. doi: 10.1038/s41467-018-06075-7. PMID:30190470<ref>PMID:30190470</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6a69" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Calcium-transporting ATPase]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Chi, X M]] | |||
[[Category: Gong, D S]] | |||
[[Category: Huang, G X.Y]] | |||
[[Category: Lei, J L]] | |||
[[Category: Ren, K]] | |||
[[Category: Yan, N]] | |||
[[Category: Zhou, G W]] | |||
[[Category: Zhou, Q]] | |||
[[Category: Membrane protein]] | |||
[[Category: Structural protein]] | |||
Revision as of 22:43, 19 September 2018
Cryo-EM structure of a P-type ATPaseCryo-EM structure of a P-type ATPase
Structural highlights
Function[AT2B1_HUMAN] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. [NPTN_HUMAN] Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). Publication Abstract from PubMedPlasma membrane Ca(2+)-ATPases (PMCAs) are key regulators of global Ca(2+) homeostasis and local intracellular Ca(2+) dynamics. Recently, Neuroplastin (NPTN) and basigin were identified as previously unrecognized obligatory subunits of PMCAs that dramatically increase the efficiency of PMCA-mediated Ca(2+) clearance. Here, we report the cryo-EM structure of human PMCA1 (hPMCA1) in complex with NPTN at a resolution of 4.1 A for the overall structure and 3.9 A for the transmembrane domain. The single transmembrane helix of NPTN interacts with the TM8-9-linker and TM10 of hPMCA1. The subunits are required for the hPMCA1 functional activity. The NPTN-bound hPMCA1 closely resembles the E1-Mg(2+) structure of endo(sarco)plasmic reticulum Ca(2+) ATPase and the Ca(2+) site is exposed through a large open cytoplasmic pathway. This structure provides insight into how the subunits bind to the PMCAs and serves as an important basis for understanding the functional mechanisms of this essential calcium pump family. Structure of the human plasma membrane Ca(2+)-ATPase 1 in complex with its obligatory subunit neuroplastin.,Gong D, Chi X, Ren K, Huang G, Zhou G, Yan N, Lei J, Zhou Q Nat Commun. 2018 Sep 6;9(1):3623. doi: 10.1038/s41467-018-06075-7. PMID:30190470[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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