{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T00:39:51Z","timestamp":1782952791698,"version":"3.54.5"},"reference-count":50,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2024,7,29]],"date-time":"2024-07-29T00:00:00Z","timestamp":1722211200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM133325"],"award-info":[{"award-number":["R35GM133325"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2024,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Rhodanese\u2010like 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\u2013sulfur cluster biogenesis, and thio\u2010cofactor biosynthesis. However, due to the inherent complexity of sulfur metabolism caused by the intrinsically high nucleophilicity and redox sensitivity of thiol\u2010containing compounds, the physiological functions of many RLDs remain to be explored. Here, we focus on a single domain <jats:italic>Acinetobacter baumannii<\/jats:italic> RLD (Ab\u2010RLD) associated with a desulfurase encapsulin which is able to store substantial amounts of sulfur inside its protein shell. We determine the 1.6\u2009\u00c5 x\u2010ray crystal structure of Ab\u2010RLD, highlighting a homodimeric structure with a number of unusual features. We show through kinetic analysis that Ab\u2010RLD exhibits thiosulfate sulfurtransferase activity with both cyanide and glutathione acceptors. Using native mass spectrometry and in vitro assays, we provide evidence that Ab\u2010RLD 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\u2010RLD and the desulfurase encapsulin.<\/jats:p>","DOI":"10.1002\/pro.5129","type":"journal-article","created":{"date-parts":[[2024,7,29]],"date-time":"2024-07-29T08:45:12Z","timestamp":1722242712000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Structural and biochemical characterization of an encapsulin\u2010associated rhodanese from <i>Acinetobacter baumannii<\/i>"],"prefix":"10.1002","volume":"33","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0612-7606","authenticated-orcid":false,"given":"Robert","family":"Benisch","sequence":"first","affiliation":[{"name":"Program in Chemical Biology University of Michigan  Ann Arbor Michigan USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6328-2031","authenticated-orcid":false,"given":"Tobias W.","family":"Giessen","sequence":"additional","affiliation":[{"name":"Program in Chemical Biology University of Michigan  Ann Arbor Michigan USA"},{"name":"Department of Biological Chemistry University of Michigan Medical School  Ann Arbor Michigan 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