View source for 7r0g


==STRUCTURAL BASIS OF ION UPTAKE IN COPPER-TRANSPORTING P1B-TYPE ATPASES==
<StructureSection load='7r0g' size='340' side='right'caption='[[7r0g]], [[Resolution|resolution]] 4.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7r0g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R0G 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]] 4.01&#8491;</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=7r0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r0g OCA], [https://pdbe.org/7r0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r0g RCSB], [https://www.ebi.ac.uk/pdbsum/7r0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r0g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A117KM49_ARCFL A0A117KM49_ARCFL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Copper is essential for living cells, yet toxic at elevated concentrations. Class 1B P-type (P1B-) ATPases are present in all kingdoms of life, facilitating cellular export of transition metals including copper. P-type ATPases follow an alternating access mechanism, with inward-facing E1 and outward-facing E2 conformations. Nevertheless, no structural information on E1 states is available for P1B-ATPases, hampering mechanistic understanding. Here, we present structures that reach 2.7 A resolution of a copper-specific P1B-ATPase in an E1 conformation, with complementing data and analyses. Our efforts reveal a domain arrangement that generates space for interaction with ion donating chaperones, and suggest a direct Cu(+) transfer to the transmembrane core. A methionine serves a key role by assisting the release of the chaperone-bound ion and forming a cargo entry site together with the cysteines of the CPC signature motif. Collectively, the findings provide insights into P1B-mediated transport, likely applicable also to human P1B-members.

Structural basis of ion uptake in copper-transporting P1B-type ATPases.,Salustros N, Gronberg C, Abeyrathna NS, Lyu P, Oradd F, Wang K, Andersson M, Meloni G, Gourdon P Nat Commun. 2022 Aug 31;13(1):5121. doi: 10.1038/s41467-022-32751-w. PMID:36045128<ref>PMID:36045128</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7r0g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Large Structures]]
[[Category: Gourdon P]]
[[Category: Groenberg C]]
[[Category: Salustros N]]
[[Category: Wang K]]