2MOI

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

Summary for 2MOI

• Entry DOI: 10.2210/pdb2moi/pdb
• Related: 2moj 2mol
• NMR Information: BMRB: 19943
• Descriptor: Inner membrane protein YgaP (1 entity in total)
• Functional Keywords: rhodanese domain, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P55734
• Total number of polymer chains: 1
• Total formula weight: 11716.31

Authors

Eichmann, C.,Tzitzilonis, C.,Bordignon, E.,Maslennikov, I.,Choe, S.,Riek, R. (deposition date: 2014-04-26, release date: 2014-06-25, Last modification date: 2024-05-01)

Primary citation

Eichmann, C.,Tzitzilonis, C.,Bordignon, E.,Maslennikov, I.,Choe, S.,Riek, R.
Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli.
J.Biol.Chem., 289:23482-23503, 2014

PubMed Abstract: 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.

PubMed: 24958726
DOI: 10.1074/jbc.M114.571935

Experimental method

SOLUTION NMR