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• W2094536364 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 Å resolution. The two proteins are covalently linked via a mixed disulfide that forms during nucleophilic attack of Trx's N-terminal cysteine on the Sγ atom of the PAPS reductase S-sulfocysteine (E-Cys-Sγ-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 Sγ 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." @default.
• W2094536364 created "2016-06-24" @default.
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• W2094536364 creator A5071803873 @default.
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• W2094536364 date "2007-03-13" @default.
• W2094536364 modified "2023-10-18" @default.
• W2094536364 title "3‘-Phosphoadenosine-5‘-phosphosulfate Reductase in Complex with Thioredoxin: A Structural Snapshot in the Catalytic Cycle^," @default.
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• W2094536364 doi "https://doi.org/10.1021/bi700130e" @default.
• W2094536364 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3109433" @default.
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• W2094536364 hasPublicationYear "2007" @default.
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