title: Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP.
abstract: Rhodanese domains are abundant structural modules that catalyze the transfer of a sulfur atom from thiolsulfates to cyanide via formation of a covalent persulfide intermediate that is bound to an essential conserved cysteine residue. In this study, the three-dimensional structure of the rhodanese domain of YgaP from Escherichia coli was determined using solution NMR. A typical rhodanese domain fold was observed, as expected from the high homology with the catalytic domain of other sulfur transferases. The initial sulfur-transfer step and formation of the rhodanese persulfide intermediate were monitored by addition of sodium thiosulfate using two-dimensional (1)H-(15)N correlation spectroscopy. Discrete sharp signals were observed upon substrate addition, indicting fast exchange between sulfur-free and persulfide-intermediate forms. Residues exhibiting pronounced chemical shift changes were mapped to the structure, and included both substrate binding and surrounding residues.
authors.affiliation: Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Wei
authors.initials: W
authors.lastname: Wang
authors.affiliation: High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, PR China.
authors.forename: Peng
authors.initials: P
authors.lastname: Zhou
authors.affiliation: Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Yao
authors.initials: Y
authors.lastname: He
authors.affiliation: Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Lu
authors.initials: L
authors.lastname: Yu
authors.affiliation: Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Xiong
authors.affiliation: Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China; High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, PR China. Electronic address: cltian@ustc.edu.cn.
authors.forename: Changlin
authors.initials: C
authors.lastname: Tian
authors.affiliation: High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, PR China. Electronic address: fmwu@hmfl.ac.cn.
authors.forename: Fangming
authors.initials: F
authors.lastname: Wu
mesh_terms: D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry* / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D007700:Kinetics; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040681:Structural Homology, Protein; D013379:Substrate Specificity; D013440:Sulfides / Q000737:chemistry* / Q000378:metabolism; D013455:Sulfur / Q000737:chemistry* / Q000378:metabolism; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013885:Thiosulfates / Q000737:chemistry
chemical_list: D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D013440:Sulfides; D013885:Thiosulfates; C530142:YgaP protein, E coli; C051552:persulfides; D013455:Sulfur; D013884:Thiosulfate Sulfurtransferase; C017717:sodium thiosulfate; D003545:Cysteine
keywords: Chemical shift perturbation; Fast conformational exchange; Rhodanese domain; Solution NMR; Sulfur transfer; Three-dimensional structure