8q75: Difference between revisions

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'''Unreleased structure'''


The entry 8q75 is ON HOLD  until Paper Publication
==Copper-transporting ATPase HMA4 in E2P state with AlF==
<StructureSection load='8q75' size='340' side='right'caption='[[8q75]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8q75]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q75 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</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=8q75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q75 OCA], [https://pdbe.org/8q75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q75 RCSB], [https://www.ebi.ac.uk/pdbsum/8q75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q75 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Copper transporting P-type (P(1B-1)-) ATPases are essential for cellular homeostasis. Nonetheless, the E1-E1P-E2P-E2 states mechanism of P(1B-1)-ATPases remains poorly understood. In particular, the role of the intrinsic metal binding domains (MBDs) is enigmatic. Here, four cryo-EM structures and molecular dynamics simulations of a P(1B-1)-ATPase are combined to reveal that in many eukaryotes the MBD immediately prior to the ATPase core, MBD(-1), serves a structural role, remodeling the ion-uptake region. In contrast, the MBD prior to MBD(-1), MBD(-2), likely assists in copper delivery to the ATPase core. Invariant Tyr, Asn and Ser residues in the transmembrane domain assist in positioning sulfur-providing copper-binding amino acids, allowing for copper uptake, binding and release. As such, our findings unify previously conflicting data on the transport and regulation of P(1B-1)-ATPases. The results are critical for a fundamental understanding of cellular copper homeostasis and for comprehension of the molecular bases of P(1B-1)-disorders and ongoing clinical trials.


Authors:  
Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases.,Guo Z, Oradd F, Bagenholm V, Gronberg C, Ma JF, Ott P, Wang Y, Andersson M, Pedersen PA, Wang K, Gourdon P Nat Commun. 2024 Mar 27;15(1):2690. doi: 10.1038/s41467-024-47001-4. PMID:38538615<ref>PMID:38538615</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8q75" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryza sativa Japonica Group]]
[[Category: Gourdon P]]
[[Category: Guo Z]]
[[Category: Wang K]]

Latest revision as of 07:03, 3 July 2025

Copper-transporting ATPase HMA4 in E2P state with AlF

8q75, resolution 3.20Å

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