FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2784974269> ?p ?o ?g. }

• W2784974269 endingPage "2686" @default.
• W2784974269 startingPage "2675" @default.
• W2784974269 abstract "Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats, or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known. Mammalian rhodanese and mercaptopyruvate sulfurtransferase are perhaps the best-studied members of this protein superfamily and are involved in hydrogen sulfide metabolism. The relatively unstudied human thiosulfate sulfurtransferase-like domain–containing 1 (TSTD1) protein, a single-domain cytoplasmic sulfurtransferase, was also postulated to play a role in the sulfide oxidation pathway using thiosulfate to form glutathione persulfide, for subsequent processing in the mitochondrial matrix. Prior kinetic analysis of TSTD1 was performed at pH 9.2, raising questions about relevance and the proposed model for TSTD1 function. In this study, we report a 1.04 Å resolution crystal structure of human TSTD1, which displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase. Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low Km for thioredoxin as a sulfane sulfur acceptor and that it utilizes thiosulfate inefficiently as a sulfur donor. The active site exposure and its interaction with thioredoxin suggest that TSTD1 might play a role in sulfide-based signaling. The apical localization of TSTD1 in human colonic crypts, which interfaces with sulfide-releasing microbes, and the overexpression of TSTD1 in colon cancer provide potentially intriguing clues as to its role in sulfide metabolism. Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats, or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known. Mammalian rhodanese and mercaptopyruvate sulfurtransferase are perhaps the best-studied members of this protein superfamily and are involved in hydrogen sulfide metabolism. The relatively unstudied human thiosulfate sulfurtransferase-like domain–containing 1 (TSTD1) protein, a single-domain cytoplasmic sulfurtransferase, was also postulated to play a role in the sulfide oxidation pathway using thiosulfate to form glutathione persulfide, for subsequent processing in the mitochondrial matrix. Prior kinetic analysis of TSTD1 was performed at pH 9.2, raising questions about relevance and the proposed model for TSTD1 function. In this study, we report a 1.04 Å resolution crystal structure of human TSTD1, which displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase. Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low Km for thioredoxin as a sulfane sulfur acceptor and that it utilizes thiosulfate inefficiently as a sulfur donor. The active site exposure and its interaction with thioredoxin suggest that TSTD1 might play a role in sulfide-based signaling. The apical localization of TSTD1 in human colonic crypts, which interfaces with sulfide-releasing microbes, and the overexpression of TSTD1 in colon cancer provide potentially intriguing clues as to its role in sulfide metabolism." @default.
• W2784974269 created "2018-02-02" @default.
• W2784974269 creator A5003268449 @default.
• W2784974269 creator A5013907641 @default.
• W2784974269 creator A5042790775 @default.
• W2784974269 creator A5075652120 @default.
• W2784974269 creator A5083355596 @default.
• W2784974269 creator A5089769365 @default.
• W2784974269 creator A5091848020 @default.
• W2784974269 date "2018-02-01" @default.
• W2784974269 modified "2023-10-18" @default.
• W2784974269 title "Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin" @default.
• W2784974269 cites W1131085297 @default.
• W2784974269 cites W1481536411 @default.
• W2784974269 cites W1512796251 @default.
• W2784974269 cites W1515263113 @default.
• W2784974269 cites W1560699403 @default.
• W2784974269 cites W1963570235 @default.
• W2784974269 cites W1968209620 @default.
• W2784974269 cites W1968855741 @default.
• W2784974269 cites W1984706424 @default.
• W2784974269 cites W1986619660 @default.
• W2784974269 cites W1994515949 @default.
• W2784974269 cites W2001444438 @default.
• W2784974269 cites W2002360764 @default.
• W2784974269 cites W2009419813 @default.
• W2784974269 cites W2012794505 @default.
• W2784974269 cites W2015028228 @default.
• W2784974269 cites W2017048422 @default.
• W2784974269 cites W2021029508 @default.
• W2784974269 cites W2029582401 @default.
• W2784974269 cites W2033017235 @default.
• W2784974269 cites W2039937164 @default.
• W2784974269 cites W2041867306 @default.
• W2784974269 cites W2047399603 @default.
• W2784974269 cites W2049504582 @default.
• W2784974269 cites W2051924152 @default.
• W2784974269 cites W2054064167 @default.
• W2784974269 cites W2057902040 @default.
• W2784974269 cites W2065118166 @default.
• W2784974269 cites W2069795071 @default.
• W2784974269 cites W2072096428 @default.
• W2784974269 cites W2072540192 @default.
• W2784974269 cites W2077136939 @default.
• W2784974269 cites W2079213411 @default.
• W2784974269 cites W2079250193 @default.
• W2784974269 cites W2079632567 @default.
• W2784974269 cites W2080562319 @default.
• W2784974269 cites W2082248564 @default.
• W2784974269 cites W2088332099 @default.
• W2784974269 cites W2107312159 @default.
• W2784974269 cites W2122753552 @default.
• W2784974269 cites W2125625153 @default.
• W2784974269 cites W2127347907 @default.
• W2784974269 cites W2141610173 @default.
• W2784974269 cites W2144081223 @default.
• W2784974269 cites W2144215775 @default.
• W2784974269 cites W2151537993 @default.
• W2784974269 cites W2154714625 @default.
• W2784974269 cites W2156076210 @default.
• W2784974269 cites W2163168736 @default.
• W2784974269 cites W2163627465 @default.
• W2784974269 cites W2165565773 @default.
• W2784974269 cites W2169746496 @default.
• W2784974269 cites W2180229411 @default.
• W2784974269 cites W2239849371 @default.
• W2784974269 cites W2256535334 @default.
• W2784974269 cites W2272736396 @default.
• W2784974269 cites W2407469013 @default.
• W2784974269 cites W2415654683 @default.
• W2784974269 cites W2727010808 @default.
• W2784974269 cites W4248872320 @default.
• W2784974269 cites W993665042 @default.
• W2784974269 doi "https://doi.org/10.1074/jbc.ra117.000826" @default.
• W2784974269 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5827441" @default.
• W2784974269 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29348167" @default.
• W2784974269 hasPublicationYear "2018" @default.
• W2784974269 type Work @default.
• W2784974269 sameAs 2784974269 @default.
• W2784974269 citedByCount "44" @default.
• W2784974269 countsByYear W27849742692018 @default.
• W2784974269 countsByYear W27849742692019 @default.
• W2784974269 countsByYear W27849742692020 @default.
• W2784974269 countsByYear W27849742692021 @default.
• W2784974269 countsByYear W27849742692022 @default.
• W2784974269 countsByYear W27849742692023 @default.
• W2784974269 crossrefType "journal-article" @default.
• W2784974269 hasAuthorship W2784974269A5003268449 @default.
• W2784974269 hasAuthorship W2784974269A5013907641 @default.
• W2784974269 hasAuthorship W2784974269A5042790775 @default.
• W2784974269 hasAuthorship W2784974269A5075652120 @default.
• W2784974269 hasAuthorship W2784974269A5083355596 @default.
• W2784974269 hasAuthorship W2784974269A5089769365 @default.
• W2784974269 hasAuthorship W2784974269A5091848020 @default.
• W2784974269 hasBestOaLocation W27849742691 @default.
• W2784974269 hasConcept C178790620 @default.
• W2784974269 hasConcept C181199279 @default.
• W2784974269 hasConcept C185592680 @default.

• next