8W14
Rhodanese-like domain from Acinetobacter baumannii 118362
Summary for 8W14
| Entry DOI | 10.2210/pdb8w14/pdb |
| Descriptor | Rhodanese, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | thiosulfate sulfurtransferase, rhodanese, sulfur trafficking, single domain rhodanese, transferase |
| Biological source | Acinetobacter baumannii 118362 |
| Total number of polymer chains | 2 |
| Total formula weight | 38698.24 |
| Authors | |
| Primary citation | Benisch, R.,Giessen, T.W. Structural and biochemical characterization of an encapsulin-associated rhodanese from Acinetobacter baumannii. Protein Sci., 33:e5129-e5129, 2024 Cited by PubMed Abstract: Rhodanese-like domains (RLDs) represent a widespread protein family canonically involved in sulfur transfer reactions between diverse donor and acceptor molecules. RLDs mediate these transsulfuration reactions via a transient persulfide intermediate, created by modifying a conserved cysteine residue in their active sites. RLDs are involved in various aspects of sulfur metabolism, including sulfide oxidation in mitochondria, iron-sulfur cluster biogenesis, and thio-cofactor biosynthesis. However, due to the inherent complexity of sulfur metabolism caused by the intrinsically high nucleophilicity and redox sensitivity of thiol-containing compounds, the physiological functions of many RLDs remain to be explored. Here, we focus on a single domain Acinetobacter baumannii RLD (Ab-RLD) associated with a desulfurase encapsulin which is able to store substantial amounts of sulfur inside its protein shell. We determine the 1.6 Å x-ray crystal structure of Ab-RLD, highlighting a homodimeric structure with a number of unusual features. We show through kinetic analysis that Ab-RLD exhibits thiosulfate sulfurtransferase activity with both cyanide and glutathione acceptors. Using native mass spectrometry and in vitro assays, we provide evidence that Ab-RLD can stably carry a persulfide and thiosulfate modification and may employ a ternary catalytic mechanism. Our results will inform future studies aimed at investigating the functional link between Ab-RLD and the desulfurase encapsulin. PubMed: 39073218DOI: 10.1002/pro.5129 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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