4Y2K

reduced form of apo-GolB

Summary for 4Y2K

• Entry DOI: 10.2210/pdb4y2k/pdb
• Related: 4Y2I 4Y2M
• Descriptor: Putative metal-binding transport protein (2 entities in total)
• Functional Keywords: redued form, gold binding protein, metal transport
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Total number of polymer chains: 1
• Total formula weight: 6927.87

Authors

Wei, W.,Wang, F.,Ma, L.,Zhao, J. (deposition date: 2015-02-10, release date: 2016-02-10, Last modification date: 2024-03-20)

Primary citation

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., 137:15358-15361, 2015

PubMed Abstract: 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 (∼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.

PubMed: 26636614
DOI: 10.1021/jacs.5b09895

Experimental method

X-RAY DIFFRACTION (1.7 Å)