Structure analysis of yeast glutaredoxin Grx6 protein produced in Escherichia coli.

ABSTRACT:

Background

Grx6 is a yeast Golgi/endoplasmic reticulum protein involved in iron-sulfur binding that belongs to monothiol glutaredoxin-protein family. Grx6 has been biochemically characterized previously. Grx6 contains a conserved cysteine residue (Cys-136). Depending on the active-site sequences, Grxs can be classified to classic dithiol Grxs with a CXXC motif known as classes II and monothiol Grxs with a CXXS motif known as classes I, and Grx6 belongs to the class I with a CSYS motif.

Results

Our results showed how the loop between the N-terminal and C-terminal can affect the stability. When Grx6 was incubated with FeSO₄·7H₂O and (NH₄)₂Fe(SO₄)₂·6H₂O, a disulfide bond was formed between the cysteine

SUBMITTER: Abdalla M 

PROVIDER: S-EPMC6091153 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature