2MRM

Solution structure of the rhodanese domain of YgaP from E. coli

Summary for 2MRM

• Entry DOI: 10.2210/pdb2mrm/pdb
• NMR Information: BMRB: 25085
• Descriptor: Membrane protein (1 entity in total)
• Functional Keywords: rhodanese domain, ygap, e. coli, integral membrane protein, membrane protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12620.39

Authors

Wang, W.,Zhou, P.,Tian, C.,Wu, F. (deposition date: 2014-07-12, release date: 2014-10-08, Last modification date: 2024-05-01)

Primary citation

Wang, W.,Zhou, P.,He, Y.,Yu, L.,Xiong, Y.,Tian, C.,Wu, F.
Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP
Biochem.Biophys.Res.Commun., 452:817-821, 2014

PubMed 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.

PubMed: 25204500
DOI: 10.1016/j.bbrc.2014.09.002

Experimental method

SOLUTION NMR