2xla: Difference between revisions
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< | ==Structure and metal-loading of a soluble periplasm cupro-protein: Cu- CucA-closed== | ||
<StructureSection load='2xla' size='340' side='right'caption='[[2xla]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xla]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XLA 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]] 1.93Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=URE:UREA'>URE</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=2xla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xla OCA], [https://pdbe.org/2xla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xla RCSB], [https://www.ebi.ac.uk/pdbsum/2xla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xla ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P73600_SYNY3 P73600_SYNY3] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/2xla_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2xla ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A copper-trafficking pathway was found to enable Cu(2+) occupancy of a soluble periplasm protein, CucA, even when competing Zn(2+) is abundant in the periplasm. Here, we solved the structure of CucA (a new cupin) and found that binding of Cu(2+), but not Zn(2+), quenches the fluorescence of Trp(165), which is adjacent to the metal site. Using this fluorescence probe, we established that CucA becomes partly occupied by Zn(2+) following exposure to equimolar Zn(2+) and Cu(2+). Cu(2+)-CucA is more thermodynamically stable than Zn(2+)-CucA but k((Zn-->Cu)exchange) is slow, raising questions about how the periplasm contains solely the Cu(2+) form. We discovered that a copper-trafficking pathway involving two copper transporters (CtaA and PacS) and a metallochaperone (Atx1) is obligatory for Cu(2+)-CucA to accumulate in the periplasm. There was negligible CucA protein in the periplasm of DeltactaA cells, but the abundance of cucA transcripts was unaltered. Crucially, DeltactaA cells overaccumulate low M(r) copper complexes in the periplasm, and purified apoCucA can readily acquire Cu(2+) from DeltactaA periplasm extracts, but in vivo apoCucA fails to come into contact with these periplasmic copper pools. Instead, copper traffics via a cytoplasmic pathway that is coupled to CucA translocation to the periplasm. | |||
Structure and metal loading of a soluble periplasm cuproprotein.,Waldron KJ, Firbank SJ, Dainty SJ, Perez-Rama M, Tottey S, Robinson NJ J Biol Chem. 2010 Oct 15;285(42):32504-11. Epub 2010 Aug 10. PMID:20702411<ref>PMID:20702411</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xla" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Synechocystis sp. PCC 6803]] | |||
[[Category: Dainty SJ]] | |||
== | [[Category: Firbank SJ]] | ||
< | [[Category: Perez-Rama M]] | ||
[[Category: Synechocystis sp. | [[Category: Robinson NJ]] | ||
[[Category: Dainty | [[Category: Tottey S]] | ||
[[Category: Firbank | [[Category: Waldron KJ]] | ||
[[Category: Perez-Rama | |||
[[Category: Robinson | |||
[[Category: Tottey | |||
[[Category: Waldron | |||
Latest revision as of 13:33, 20 December 2023
Structure and metal-loading of a soluble periplasm cupro-protein: Cu- CucA-closedStructure and metal-loading of a soluble periplasm cupro-protein: Cu- CucA-closed
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA copper-trafficking pathway was found to enable Cu(2+) occupancy of a soluble periplasm protein, CucA, even when competing Zn(2+) is abundant in the periplasm. Here, we solved the structure of CucA (a new cupin) and found that binding of Cu(2+), but not Zn(2+), quenches the fluorescence of Trp(165), which is adjacent to the metal site. Using this fluorescence probe, we established that CucA becomes partly occupied by Zn(2+) following exposure to equimolar Zn(2+) and Cu(2+). Cu(2+)-CucA is more thermodynamically stable than Zn(2+)-CucA but k((Zn-->Cu)exchange) is slow, raising questions about how the periplasm contains solely the Cu(2+) form. We discovered that a copper-trafficking pathway involving two copper transporters (CtaA and PacS) and a metallochaperone (Atx1) is obligatory for Cu(2+)-CucA to accumulate in the periplasm. There was negligible CucA protein in the periplasm of DeltactaA cells, but the abundance of cucA transcripts was unaltered. Crucially, DeltactaA cells overaccumulate low M(r) copper complexes in the periplasm, and purified apoCucA can readily acquire Cu(2+) from DeltactaA periplasm extracts, but in vivo apoCucA fails to come into contact with these periplasmic copper pools. Instead, copper traffics via a cytoplasmic pathway that is coupled to CucA translocation to the periplasm. Structure and metal loading of a soluble periplasm cuproprotein.,Waldron KJ, Firbank SJ, Dainty SJ, Perez-Rama M, Tottey S, Robinson NJ J Biol Chem. 2010 Oct 15;285(42):32504-11. Epub 2010 Aug 10. PMID:20702411[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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