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

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.
Authors:
 [1] ;  [2] ; ; ;  [1] ;  [1] ;  [3] ;  [2]
  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)
  3. (China)
Publication Date:
OSTI Identifier:
22416760
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 452; Journal Issue: 3; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
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