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Solution NMR structure and functional analysis of the integral membrane protein YgaP from Escherichia coli.

J. Biol. Chem.2014 Aug 22;289(34):23482-503. Epub 2014 Jun 23
Cédric Eichmann 1 , Christos Tzitzilonis 2 , Enrica Bordignon 1 , Innokentiy Maslennikov 3 , Senyon Choe 3 , Roland Riek 4
Cédric Eichmann 1 , Christos Tzitzilonis 2 , Enrica Bordignon 1 , Innokentiy Maslennikov 3 , Senyon Choe 3 , Roland Riek 4
+ et al

[No authors listed]

Author information
  • 1 From the Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland and.
  • 2 From the Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland and the Structural Biology Laboratory, The Salk Institute, La Jolla, California 92037.
  • 3 the Structural Biology Laboratory, The Salk Institute, La Jolla, California 92037.
  • 4 From the Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland and the Structural Biology Laboratory, The Salk Institute, La Jolla, California 92037 roland.riek@phys.chem.ethz.ch.

摘要


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. © 2014 by The American Society for Biochemistry and Inc.

KEYWORDS: Enzyme Catalysis, Membrane Enzyme, Membrane Protein, Nuclear Magnetic Resonance (NMR), Rhodanese, Structural Biology, Sulfotransferase, Sulfurtransferase, Three-dimensional Structure