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| | <StructureSection load='4y2m' size='340' side='right'caption='[[4y2m]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='4y2m' size='340' side='right'caption='[[4y2m]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y2m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y2M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y2M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y2m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y2M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y2i|4y2i]], [[4y2k|4y2k]]</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=4y2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2m OCA], [https://pdbe.org/4y2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y2m RCSB], [https://www.ebi.ac.uk/pdbsum/4y2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2m ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STMDT2_03511 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</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=4y2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2m OCA], [http://pdbe.org/4y2m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y2m RCSB], [http://www.ebi.ac.uk/pdbsum/4y2m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A140UHB4_SALTM A0A140UHB4_SALTM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhimurium loeffler 1892]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Wang, F]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Wei, W]] | + | [[Category: Wang F]] |
| - | [[Category: Zhao, J]] | + | [[Category: Wei W]] |
| - | [[Category: Gold binding protein]] | + | [[Category: Zhao J]] |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Oxidized form]]
| + | |
| Structural highlights
Function
A0A140UHB4_SALTM
Publication Abstract from PubMed
The coordination bond between gold and sulfur (Au-S) has been widely studied and utilized in many fields. However, detailed investigations on the basic nature of this bond are still lacking. A gold-specific binding protein, GolB, was recently identified, providing a unique opportunity for the study of the Au-S bond at the molecular level. We probed the mechanical strength of the gold-sulfur bond in GolB using single-molecule force spectroscopy. We measured the rupture force of the Au-S bond to be 165 pN, much lower than Au-S bonds measured on different gold surfaces ( approximately 1000 pN). We further solved the structures of apo-GolB and Au(I)-GolB complex using X-ray crystallography. These structures showed that the average Au-S bond length in GolB is much longer than the reported average value of Au-S bonds. Our results highlight the dramatic influence of the unique biological environment on the stability and strength of metal coordination bonds in proteins.
Structural Insights and the Surprisingly Low Mechanical Stability of the Au-S Bond in the Gold-Specific Protein GolB.,Wei W, Sun Y, Zhu M, Liu X, Sun P, Wang F, Gui Q, Meng W, Cao Y, Zhao J J Am Chem Soc. 2015 Dec 16;137(49):15358-61. doi: 10.1021/jacs.5b09895. Epub 2015, Dec 4. PMID:26636614[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wei W, Sun Y, Zhu M, Liu X, Sun P, Wang F, Gui Q, Meng W, Cao Y, Zhao J. Structural Insights and the Surprisingly Low Mechanical Stability of the Au-S Bond in the Gold-Specific Protein GolB. J Am Chem Soc. 2015 Dec 16;137(49):15358-61. doi: 10.1021/jacs.5b09895. Epub 2015, Dec 4. PMID:26636614 doi:http://dx.doi.org/10.1021/jacs.5b09895
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