Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP

Journal Article · Fri Sep 26 04:00:00 EDT 2014 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/J.BBRC.2014.09.002· OSTI ID:22416760

Wang, Wei ^[1]; Zhou, Peng ^[2]; He, Yao; Yu, Lu; Xiong, Ying ^[1]; Tian, Changlin ^[1]; Wu, Fangming ^[2]

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1. Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026 (China)
2. High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031 (China)

Highlights: • Three dimensional solution NMR structure of YgaP rhodanese domain. • Function validation of YgaP rhodanese domain to substrate Na{sub 2}S{sub 2}O{sub 3}. • Fast exchange between the intact and persulfide-intermediate rhodanese domain. - 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 {sup 1}H–{sup 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.

• OSTI ID: 22416760
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 3 Vol. 452; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CHEMICAL SHIFT
COVALENCE
CYANIDES
CYSTEINE
ESCHERICHIA COLI
HYDROGEN 1
NITROGEN 15
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
RESIDUES
SODIUM SULFATES
SUBSTRATES
TRANSFERASES