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| | ==CRYSTAL STRUCTURE OF A ZINC-TRANSPORTING PIB-TYPE ATPASE IN THE E2P STATE== | | ==CRYSTAL STRUCTURE OF A ZINC-TRANSPORTING PIB-TYPE ATPASE IN THE E2P STATE== |
| - | <StructureSection load='4umv' size='340' side='right' caption='[[4umv]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='4umv' size='340' side='right'caption='[[4umv]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4umv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UMV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4umv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_sonnei Shigella sonnei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UMV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4umw|4umw]]</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=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Zinc-exporting_ATPase Zinc-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.5 3.6.3.5] </span></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=4umv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4umv OCA], [https://pdbe.org/4umv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4umv RCSB], [https://www.ebi.ac.uk/pdbsum/4umv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4umv ProSAT]</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=4umv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4umv OCA], [http://pdbe.org/4umv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4umv RCSB], [http://www.ebi.ac.uk/pdbsum/4umv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4umv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ZNTA_SHISS ZNTA_SHISS] Confers resistance to zinc, cadmium and lead. Couples the hydrolysis of ATP with the export of zinc, cadmium or lead.<ref>PMID:25132545</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[ATPase|ATPase]] | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Zinc-exporting ATPase]] | + | [[Category: Large Structures]] |
| - | [[Category: Andersson, M]] | + | [[Category: Shigella sonnei]] |
| - | [[Category: Autzen, H E]] | + | [[Category: Andersson M]] |
| - | [[Category: Gourdon, P]] | + | [[Category: Autzen HE]] |
| - | [[Category: Klymchuk, T]] | + | [[Category: Gourdon P]] |
| - | [[Category: Meloni, G]] | + | [[Category: Klymchuk T]] |
| - | [[Category: Nielsen, A M]] | + | [[Category: Meloni G]] |
| - | [[Category: Nissen, P]] | + | [[Category: Nielsen AM]] |
| - | [[Category: Rees, D C]] | + | [[Category: Nissen P]] |
| - | [[Category: Sitsel, O]] | + | [[Category: Rees DC]] |
| - | [[Category: Wang, K T]] | + | [[Category: Sitsel O]] |
| - | [[Category: Atp-binding]]
| + | [[Category: Wang KT]] |
| - | [[Category: Cpc]]
| + | |
| - | [[Category: Cxxc]]
| + | |
| - | [[Category: Heavy-metal binding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: P-type atpase]]
| + | |
| - | [[Category: Pi-atpase]]
| + | |
| - | [[Category: Pib-atpase]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Zinc transport]]
| + | |
| - | [[Category: Zn2+ exporting]]
| + | |
| Structural highlights
Function
ZNTA_SHISS Confers resistance to zinc, cadmium and lead. Couples the hydrolysis of ATP with the export of zinc, cadmium or lead.[1]
Publication Abstract from PubMed
Zinc is an essential micronutrient for all living organisms. It is required for signalling and proper functioning of a range of proteins involved in, for example, DNA binding and enzymatic catalysis. In prokaryotes and photosynthetic eukaryotes, Zn2+-transporting P-type ATPases of class IB (ZntA) are crucial for cellular redistribution and detoxification of Zn2+ and related elements. Here we present crystal structures representing the phosphoenzyme ground state (E2P) and a dephosphorylation intermediate (E2.Pi) of ZntA from Shigella sonnei, determined at 3.2 A and 2.7 A resolution, respectively. The structures reveal a similar fold to Cu+-ATPases, with an amphipathic helix at the membrane interface. A conserved electronegative funnel connects this region to the intramembranous high-affinity ion-binding site and may promote specific uptake of cellular Zn2+ ions by the transporter. The E2P structure displays a wide extracellular release pathway reaching the invariant residues at the high-affinity site, including C392, C394 and D714. The pathway closes in the E2.Pi state, in which D714 interacts with the conserved residue K693, which possibly stimulates Zn2+ release as a built-in counter ion, as has been proposed for H+-ATPases. Indeed, transport studies in liposomes provide experimental support for ZntA activity without counter transport. These findings suggest a mechanistic link between PIB-type Zn2+-ATPases and PIII-type H+-ATPases and at the same time show structural features of the extracellular release pathway that resemble PII-type ATPases such as the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase (SERCA) and Na+, K+-ATPase. These findings considerably increase our understanding of zinc transport in cells and represent new possibilities for biotechnology and biomedicine.
Structure and mechanism of Zn-transporting P-type ATPases.,Wang K, Sitsel O, Meloni G, Autzen HE, Andersson M, Klymchuk T, Nielsen AM, Rees DC, Nissen P, Gourdon P Nature. 2014 Aug 17. doi: 10.1038/nature13618. PMID:25132545[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang K, Sitsel O, Meloni G, Autzen HE, Andersson M, Klymchuk T, Nielsen AM, Rees DC, Nissen P, Gourdon P. Structure and mechanism of Zn-transporting P-type ATPases. Nature. 2014 Aug 17. doi: 10.1038/nature13618. PMID:25132545 doi:http://dx.doi.org/10.1038/nature13618
- ↑ Wang K, Sitsel O, Meloni G, Autzen HE, Andersson M, Klymchuk T, Nielsen AM, Rees DC, Nissen P, Gourdon P. Structure and mechanism of Zn-transporting P-type ATPases. Nature. 2014 Aug 17. doi: 10.1038/nature13618. PMID:25132545 doi:http://dx.doi.org/10.1038/nature13618
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