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=4y2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2k OCA], [https://pdbe.org/4y2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y2k RCSB], [https://www.ebi.ac.uk/pdbsum/4y2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2k ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== 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<ref>PMID:26636614</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 4y2k" style="background-color:#fffaf0;"></div>

== References ==

<references/>