5WK0
Crystal structure of the bacillithiol transferase BstA from Staphylococcus aureus.
Summary for 5WK0
| Entry DOI | 10.2210/pdb5wk0/pdb |
| Descriptor | Damage-inducible protein DinB, NICKEL (II) ION (3 entities in total) |
| Functional Keywords | bacillithiol, detoxification, helix bundle, metalloenzyme, unknown function |
| Biological source | Staphylococcus sp. HMSC055H04 |
| Total number of polymer chains | 1 |
| Total formula weight | 18731.99 |
| Authors | Cook, P.D.,Francis, J.W. (deposition date: 2017-07-24, release date: 2018-02-21, Last modification date: 2023-10-04) |
| Primary citation | Francis, J.W.,Royer, C.J.,Cook, P.D. Structure and function of the bacillithiol-S-transferase BstA from Staphylococcus aureus. Protein Sci., 27:898-902, 2018 Cited by PubMed Abstract: Bacillithiol is a low-molecular weight thiol produced by many gram-positive organisms, including Staphylococcus aureus and Bacillus anthracis. It is the major thiol responsible for maintaining redox homeostasis and cellular detoxification, including inactivation of the antibiotic fosfomycin. The metal-dependent bacillithiol transferase BstA is likely involved in these sorts of detoxification processes, but the exact substrates and enzyme mechanism have not been identified. Here we report the 1.34 Å resolution X-ray crystallographic structure of BstA from S. aureus. Our structure confirms that BstA belongs to the YfiT-like metal-dependent hydrolase superfamily. Like YfiT, our structure contains nickel within its active site, but our functional data suggest that BstA utilizes zinc for activity. Although BstA and YfiT both contain a core four helix bundle and coordinate their metal ions in the same fashion, significant differences between the protein structures are described here. PubMed: 29417696DOI: 10.1002/pro.3384 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.335 Å) |
Structure validation
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