Thiosulfate sulfurtransferase.
MTTDASRTTSFTPAALQHLLTTGDGPRLLDVRTPGEFRTGHIPGAYNVPLDTLREHRMEL
GRHLDQDVVLVCRSGARATRAEEALAEAGLPNLRVLDGGMMAWEASGAPVNRGEQRWEME
RQVRLIAGSIVLVSGVVGFFVPGVHLIGTAIGAGLTFAALSNTCAMGMMLAKLPYNRGPR
TDIRSVIASLRNRA197
| PMID | Title & Author | Abstract | Year | |
| 0 | 24958726 | Solution NMR structure and functional analysis of the integral membrane protein YgaP from Escherichia coli. Eichmann C, Tzitzilonis C, Bordignon E, Maslennikov I, Choe S, Riek R. | The solution NMR structure of the α-helical integral membrane protein YgaP from Escherichia coli in mixed 1,2-diheptanoyl-sn-glycerol-3-phosphocholine/1-myristoyl-2-hydroxy-sn-glycero-3-phospho-(1'-rac-glycerol) micelles is presented. In these micelles, YgaP forms a homodimer with the two transmembrane helices being the dimer interface, whereas the N-terminal cytoplasmic domain includes a rhodanese-fold in accordance to its sequence homology to the rhodanese family of sulfurtransferases. The enzymatic sulfur transfer activity of full-length YgaP as well as of the N-terminal rhodanese domain only was investigated performing a series of titrations with sodium thiosulfate and potassium cyanide monitored by NMR and EPR. The data indicate the thiosulfate concentration-dependent addition of several sulfur atoms to the catalytic Cys-63, which process can be reversed by the addition of potassium cyanide. The catalytic reaction induces thereby conformational changes within the rhodanese domain, as well as on the transmembrane α-helices of YgaP. These results provide insights into a potential mechanism of YgaP during the catalytic thiosulfate activity in vivo. | 2014 |
| 1 | 25204500 | Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP . Wang W, Zhou P, He Y, Yu L, Xiong Y, Tian C, Wu F. | 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. | 2014 |
| 2 | 26817826 | Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method. Ling S, Wang W, Yu L, Peng J, Cai X, Xiong Y, Hayati Z, Zhang L, Zhang Z, Song L, Tian C. | Electron paramagnetic resonance (EPR)-based hybrid experimental and computational approaches were applied to determine the structure of a full-length E. coli integral membrane sulfurtransferase, dimeric YgaP, and its structural and dynamic changes upon ligand binding. The solution NMR structures of the YgaP transmembrane domain (TMD) and cytosolic catalytic rhodanese domain were reported recently, but the tertiary fold of full-length YgaP was not yet available. Here, systematic site-specific EPR analysis defined a helix-loop-helix secondary structure of the YagP-TMD monomers using mobility, accessibility and membrane immersion measurements. The tertiary folds of dimeric YgaP-TMD and full-length YgaP in detergent micelles were determined through inter- and intra-monomer distance mapping and rigid-body computation. Further EPR analysis demonstrated the tight packing of the two YgaP second transmembrane helices upon binding of the catalytic product SCN(-), which provides insight into the thiocyanate exportation mechanism of YgaP in the E. coli membrane. | 2016 |
Eichmann C , Tzitzilonis C , Bordignon E , et al. Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli[J]. Journal of Biological Chemistry, 2014, 289(34):23482-23503.