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| | <StructureSection load='5fig' size='340' side='right'caption='[[5fig]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5fig' size='340' side='right'caption='[[5fig]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fig]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FIG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fig]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FIG FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5arm|5arm]], [[5arn|5arn]]</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]] 1.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fig OCA], [http://pdbe.org/5fig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fig RCSB], [http://www.ebi.ac.uk/pdbsum/5fig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fig ProSAT]</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=5fig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fig OCA], [https://pdbe.org/5fig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fig RCSB], [https://www.ebi.ac.uk/pdbsum/5fig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fig ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/YHJQ_BACSU YHJQ_BACSU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Basle, A]] | + | [[Category: Basle A]] |
| - | [[Category: Dennison, C]] | + | [[Category: Dennison C]] |
| - | [[Category: Landolfi, G]] | + | [[Category: Landolfi G]] |
| - | [[Category: Platsaki, S]] | + | [[Category: Platsaki S]] |
| - | [[Category: Vita, N]] | + | [[Category: Vita N]] |
| - | [[Category: Waldron, K]] | + | [[Category: Waldron K]] |
| - | [[Category: Bacillus subtili]]
| + | |
| - | [[Category: Copper storage]]
| + | |
| - | [[Category: Copper-binding protein]]
| + | |
| Structural highlights
Function
YHJQ_BACSU
Publication Abstract from PubMed
Bacteria are thought to avoid using the essential metal ion copper in their cytosol due to its toxicity. Herein we characterize Csp3, the cytosolic member of a new family of bacterial copper storage proteins from Methylosinus trichosporium OB3b and Bacillus subtilis. These tetrameric proteins possess a large number of Cys residues that point into the cores of their four-helix bundle monomers. The Csp3 tetramers can bind a maximum of approximately 80 Cu(I) ions, mainly via thiolate groups, with average affinities in the (1-2) x 10(17) M(-1) range. Cu(I) removal from these Csp3s by higher affinity potential physiological partners and small-molecule ligands is very slow, which is unexpected for a metal-storage protein. In vivo data demonstrate that Csp3s prevent toxicity caused by the presence of excess copper. Furthermore, bacteria expressing Csp3 accumulate copper and are able to safely maintain large quantities of this metal ion in their cytosol. This suggests a requirement for storing copper in this compartment of Csp3-producing bacteria.
Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity.,Vita N, Landolfi G, Basle A, Platsaki S, Lee J, Waldron KJ, Dennison C Sci Rep. 2016 Dec 19;6:39065. doi: 10.1038/srep39065. PMID:27991525[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vita N, Landolfi G, Basle A, Platsaki S, Lee J, Waldron KJ, Dennison C. Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity. Sci Rep. 2016 Dec 19;6:39065. doi: 10.1038/srep39065. PMID:27991525 doi:http://dx.doi.org/10.1038/srep39065
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