PDBsum entry 4y2k

Metal transport

PDB id: 4y2k

Contents

Protein chain

65 a.a.

Waters ×56

PDB id:

4y2k

Name:

Metal transport

Title:

Reduced form of apo-golb

Structure:

Putative metal-binding transport protein. Chain: a. Synonym: golb. Engineered: yes

Source:

Salmonella enterica subsp. Enterica serovar typhimurium. Organism_taxid: 90371. Strain: dt2. Gene: stmdt2_03511. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.70Å R-factor: 0.206 R-free: 0.233

Authors:

W.Wei,F.Wang,L.Ma,J.Zhao

Key ref:

W.Wei et al. (2015). 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. PubMed id: 26636614 DOI: 10.1021/jacs.5b09895

Date:

10-Feb-15 Release date: 10-Feb-16

Protein chain

A0A140UHB4  (A0A140UHB4_SALTM) -  Putative metal-binding transport protein from Salmonella typhimurium

Seq: 65 a.a.

Struc: 65 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1021/jacs.5b09895

J Am Chem Soc 137:15358-15361 (2015)

PubMed id: 26636614

Structural Insights and the Surprisingly Low Mechanical Stability of the Au-S Bond in the Gold-Specific Protein GolB.

W.Wei, Y.Sun, M.Zhu, X.Liu, P.Sun, F.Wang, Q.Gui, W.Meng, Y.Cao, J.Zhao.

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.