6IOJ
Glyceraldehyde-3-phosphate dehydrogenase A (apo-form)
Summary for 6IOJ
| Entry DOI | 10.2210/pdb6ioj/pdb |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase A (2 entities in total) |
| Functional Keywords | dehydrogenase, cytosolic protein |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 1 |
| Total formula weight | 35287.10 |
| Authors | |
| Primary citation | Wang, H.,Wang, M.,Yang, X.,Xu, X.,Hao, Q.,Yan, A.,Hu, M.,Lobinski, R.,Li, H.,Sun, H. Antimicrobial silver targets glyceraldehyde-3-phosphate dehydrogenase in glycolysis ofE. coli. Chem Sci, 10:7193-7199, 2019 Cited by PubMed Abstract: Silver has long been used as an antibacterial agent, yet its molecular targets remain largely unknown. Using a custom-designed coupling of gel electrophoresis with inductively coupled plasma mass spectrometry (GE-ICP-MS), we identified six silver-binding proteins in . The majority of the identified proteins are associated with the central carbon metabolism of . Among them, we unveil that GAPDH, an essential enzyme in glycolysis, serves as a vital target of Ag in for the first time. We demonstrate that silver inhibits the enzymatic function of GAPDH through targeting Cys149 in its catalytic site. The X-ray structure reveals that Ag coordinates to Cys149 and His176 with a quasi-linear geometry (S-Ag-N angle of 157°). And unexpectedly, two Ag ions coordinate to Cys288 in the non-catalytic site with weak argentophilic interaction (Ag···Ag distance of 2.9 Å). This is the first report on antimicrobial Ag targeting a key enzyme in the glycolytic pathway of . The findings expand our knowledge on the mode of action and bio-coordination chemistry of silver, particularly silver-targeting residues in proteins at the atomic level. PubMed: 31588287DOI: 10.1039/c9sc02032b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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