ArticleBiochemistry2007
3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- The chicken gut virome: spatial structuring and extensive diversity of 19,778 viral populations.mSystems · 2026Article
- Phage-associated Cas12p nucleases require binding to bacterial thioredoxin for activation and cleavage of target DNA.Nature microbiology · 2026Article
- Distinct or Overlapping Areas of Mitochondrial Thioredoxin 2 May Be Used for Its Covalent and Strong Non-Covalent Interactions with Protein Ligands.Antioxidants (Basel, Switzerland) · 2023Article
- Article
- Metatranscriptomic Analyses Reveal the Functional Role ofJournal of fungi (Basel, Switzerland) · 2022Article
- A Genetically Encoded Fluorosulfonyloxybenzoyl-l-lysine for Expansive Covalent Bonding of Proteins via SuFEx Chemistry.Journal of the American Chemical Society · 2021Article
- Crystal Structure of the [4Fe-4S] Cluster-Containing Adenosine-5'-phosphosulfate Reductase fromACS omega · 2021Article
- Positioning Diverse Type IV Structures and Functions Within Class 1 CRISPR-Cas Systems.Frontiers in microbiology · 2021Article
- Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade.Scientific reports · 2018Article
- Interaction of Peptide Aptamers with Prion Protein Central Domain Promotes α-Cleavage of PrPMolecular neurobiology · 2018Article
- Genetically Encoding Fluorosulfate-l-tyrosine To React with Lysine, Histidine, and Tyrosine via SuFEx in Proteins in Vivo.Journal of the American Chemical Society · 2018Article
- Repurposing Auranofin, Ebselen, and PX-12 as Antimicrobial Agents Targeting the Thioredoxin System.Frontiers in microbiology · 2018Review
- Functional Site Discovery in a Sulfur Metabolism Enzyme by Using Directed Evolution.Chembiochem : a European journal of chemical biology · 2016Article
- The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.Chemical science · 2015Article
- A universal entropy-driven mechanism for thioredoxin-target recognition.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins.Frontiers in pharmacology · 2015Article
- New targets and inhibitors of mycobacterial sulfur metabolism.Infectious disorders drug targets · 2013Review
- Bifunctional electrophiles cross-link thioredoxins with redox relay partners in cells.Chemical research in toxicology · 2013Article
- ROS homeostasis during development: an evolutionary conserved strategy.Cellular and molecular life sciences : CMLS · 2012Review
- Iron-sulfur cluster engineering provides insight into the evolution of substrate specificity among sulfonucleotide reductases.ACS chemical biology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase in complex with E. coli thioredoxin 1 (Trx1) has been determined to 3.0 A resolution. The two proteins are covalently linked via a mixed disulfide that forms during nucleophilic attack of Trx's N-terminal cysteine on the Sgamma atom of the PAPS reductase S-sulfocysteine (E-Cys-Sgamma-SO3-), a central intermediate in the catalytic cycle. For the first time in a crystal structure, residues 235-244 in the PAPS reductase C-terminus are observed, depicting an array of interprotein salt bridges between Trx and the strictly conserved glutathione-like sequence, Glu238Cys239Gly240Leu241His242. The structure also reveals a Trx-binding surface adjacent to the active site cleft and regions of PAPS reductase associated with conformational change. Interaction at this site strategically positions Trx to bind the S-sulfated C-terminus and addresses the mechanism for requisite structural rearrangement of this domain. An apparent sulfite-binding pocket at the protein-protein interface explicitly orients the S-sulfocysteine Sgamma atom for nucleophilic attack in a subsequent step. Taken together, the structure of PAPS reductase in complex with Trx highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.