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Gene Review

ECs4488  -  glutaredoxin 3

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs4488

  • A set of exposed and conserved residues form a surface region, implied in glutathione binding from a known structure of E. coli Grx3 [1].
 

High impact information on ECs4488

  • Here, we use a combination of long molecular dynamics (MD) simulations, pK(a) calculations, and experimental investigations to derive the structure and dynamics of the reduced active site from Escherichia coli Grx3, and investigate the factors that stabilize the thiolate [2].
  • The structure of Grx3, in combination with the pK(a) calculations, indicate that the pK(a) of the N-terminal active-site cysteine residue in Grx3 is intermediate between that of its counterpart in DsbA and Trx [2].
 

Associations of ECs4488 with chemical compounds

  • Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed [3].

References

  1. Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli. Fladvad, M., Bellanda, M., Fernandes, A.P., Mammi, S., Vlamis-Gardikas, A., Holmgren, A., Sunnerhagen, M. J. Biol. Chem. (2005) [Pubmed]
  2. Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins. Foloppe, N., Sagemark, J., Nordstrand, K., Berndt, K.D., Nilsson, L. J. Mol. Biol. (2001) [Pubmed]
  3. NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism. Nordstrand, K., slund, F., Holmgren, A., Otting, G., Berndt, K.D. J. Mol. Biol. (1999) [Pubmed]
 
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