2MOI: 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli

The solution NMR structure of the alpha-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 alpha-helices of YgaP. These results provide insights into a potential mechanism of YgaP during the catalytic thiosulfate activity in vivo.
PDB ID: 2MOIDownload
MMDB ID: 120915
PDB Deposition Date: 2014/4/26
Updated in MMDB: 2014/09
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MOI: monomeric; determined by author
Molecular Components in 2MOI
Label Count Molecule
Protein (1 molecule)
Inner Membrane Protein Ygap(Gene symbol: ygaP)
Molecule annotation
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Citing MMDB