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| | ==NMR solution structure of ZiaAN sub mutant== | | ==NMR solution structure of ZiaAN sub mutant== |
| - | <StructureSection load='2ldi' size='340' side='right' caption='[[2ldi]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2ldi' size='340' side='right'caption='[[2ldi]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ldi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDI OCA]. <br> | + | <table><tr><td colspan='2'>[[2ldi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDI FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ofg|2ofg]], [[2ofh|2ofh]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ziaA, slr0798 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])</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=2ldi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldi OCA], [https://pdbe.org/2ldi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldi RCSB], [https://www.ebi.ac.uk/pdbsum/2ldi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldi ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | + | </table> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ldi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ldi RCSB], [http://www.ebi.ac.uk/pdbsum/2ldi PDBsum]</span></td></tr>
| + | == Function == |
| - | <table> | + | [https://www.uniprot.org/uniprot/ATZN_SYNY3 ATZN_SYNY3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.,Tottey S, Patterson CJ, Banci L, Bertini I, Felli IC, Pavelkova A, Dainty SJ, Pernil R, Waldron KJ, Foster AW, Robinson NJ Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):95-100. Epub 2011 Dec 22. PMID:22198771<ref>PMID:22198771</ref> | | Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.,Tottey S, Patterson CJ, Banci L, Bertini I, Felli IC, Pavelkova A, Dainty SJ, Pernil R, Waldron KJ, Foster AW, Robinson NJ Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):95-100. Epub 2011 Dec 22. PMID:22198771<ref>PMID:22198771</ref> |
| | | | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2ldi" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Synechocystis sp.]] | + | [[Category: Large Structures]] |
| - | [[Category: Zinc-exporting ATPase]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Banci, L.]] | + | [[Category: Banci L]] |
| - | [[Category: Bertini, I.]] | + | [[Category: Bertini I]] |
| - | [[Category: Felli, I C.]] | + | [[Category: Felli IC]] |
| - | [[Category: Pavelkova, A.]] | + | [[Category: Pavelkova A]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Metal homeostasis]]
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| - | [[Category: Metallochaperone]]
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| Structural highlights
Function
ATZN_SYNY3
Publication Abstract from PubMed
Copper metallochaperones supply copper to cupro-proteins through copper-mediated protein-protein-interactions and it has been hypothesized that metallochaperones thereby inhibit copper from causing damage en route. Evidence is presented in support of this latter role for cyanobacterial metallochaperone, Atx1. In cyanobacteria Atx1 contributes towards the supply of copper to plastocyanin inside thylakoids but it is shown here that in copper-replete medium, copper can reach plastocyanin without Atx1. Unlike metallochaperone-independent copper-supply to superoxide dismutase in eukaryotes, glutathione is not essential for Atx1-independent supply to plastocyanin: Double mutants missing atx1 and gshB (encoding glutathione synthetase) accumulate the same number of atoms of copper per cell in the plastocyanin pool as wild type. Critically, Deltaatx1DeltagshB are hypersensitive to elevated copper relative to wild type cells and also relative to DeltagshB single mutants with evidence that hypersensitivity arises due to the mislocation of copper to sites for other metals including iron and zinc. The zinc site on the amino-terminal domain (ZiaA(N)) of the P(1)-type zinc-transporting ATPase is especially similar to the copper site of the Atx1 target PacS(N), and ZiaA(N) will bind Cu(I) more tightly than zinc. An NMR model of a substituted-ZiaA(N)-Cu(I)-Atx1 heterodimer has been generated making it possible to visualize a juxtaposition of residues surrounding the ZiaA(N) zinc site, including Asp(18), which normally repulse Atx1. Equivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of P(1)-type ATPases for metals other than Cu(I) is conserved, again consistent with a role for copper metallochaperones to withhold copper from binding sites for other metals.
Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.,Tottey S, Patterson CJ, Banci L, Bertini I, Felli IC, Pavelkova A, Dainty SJ, Pernil R, Waldron KJ, Foster AW, Robinson NJ Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):95-100. Epub 2011 Dec 22. PMID:22198771[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tottey S, Patterson CJ, Banci L, Bertini I, Felli IC, Pavelkova A, Dainty SJ, Pernil R, Waldron KJ, Foster AW, Robinson NJ. Cyanobacterial metallochaperone inhibits deleterious side reactions of copper. Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):95-100. Epub 2011 Dec 22. PMID:22198771 doi:10.1073/pnas.1117515109
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