7si3: Difference between revisions
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==Consensus structure of ATP7B== | ==Consensus structure of ATP7B== | ||
<StructureSection load='7si3' size='340' side='right'caption='[[7si3]]' scene=''> | <StructureSection load='7si3' size='340' side='right'caption='[[7si3]], [[Resolution|resolution]] 3.19Å' 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=7SI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SI3 FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SI3 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=7si3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7si3 OCA], [https://pdbe.org/7si3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7si3 RCSB], [https://www.ebi.ac.uk/pdbsum/7si3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7si3 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.19Å</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=7si3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7si3 OCA], [https://pdbe.org/7si3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7si3 RCSB], [https://www.ebi.ac.uk/pdbsum/7si3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7si3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ATP7A and ATP7B, two homologous copper-transporting P1B-type ATPases, play crucial roles in cellular copper homeostasis, and mutations cause Menkes and Wilson diseases, respectively. ATP7A/B contains a P-type ATPase core consisting of a membrane transport domain and three cytoplasmic domains, the A, P, and N domains, and a unique amino terminus comprising six consecutive metal-binding domains. Here, we present a cryo-electron microscopy structure of frog ATP7B in a copper-free state. Interacting with both the A and P domains, the metal-binding domains are poised to exert copper-dependent regulation of ATP hydrolysis coupled to transmembrane copper transport. A ring of negatively charged residues lines the cytoplasmic copper entrance that is presumably gated by a conserved basic residue sitting at the center. Within the membrane, a network of copper-coordinating ligands delineates a stepwise copper transport pathway. This work provides the first glimpse into the structure and function of ATP7 proteins and facilitates understanding of disease mechanisms and development of rational therapies. | |||
Structure of the Wilson disease copper transporter ATP7B.,Bitter RM, Oh S, Deng Z, Rahman S, Hite RK, Yuan P Sci Adv. 2022 Mar 4;8(9):eabl5508. doi: 10.1126/sciadv.abl5508. Epub 2022 Mar 4. PMID:35245129<ref>PMID:35245129</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7si3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
