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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Cysteinyl and methionyl redox switches: Structural prerequisites and consequences.

Yana Bodnar1, Christopher Horst Lillig2

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Redox Biology
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PubMed
Summary

Redox modifications alter protein structures, but generally cause minor conformational changes. Specific amino acid motifs near sulfur residues may help predict these crucial protein modifications.

Keywords:
Allosteric disulfidesMethionine sulfoxidationRedox modificationsS-gluthathionylationS-nitrosylationSulfenylationThiol switches

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Redox modifications of cysteine and methionine residues are vital for regulating protein function.
  • Understanding how these modifications impact protein structure is crucial for deciphering cellular signaling pathways.

Purpose of the Study:

  • To investigate the structural effects of various oxidative modifications on proteins.
  • To identify pre-requisites and consequences of redox modifications in protein structures.

Main Methods:

  • Screening the RCSB Protein Data Bank for proteins with oxidative modifications.
  • Comparing modified protein structures with their reduced counterparts.
  • Analyzing conformational changes, electrostatic properties, and residue accessibility.

Main Results:

  • Redox modifications generally induce small conformational changes, within normal fluctuation ranges.
  • Disulfide bonds, specifically, can alter protein electrostatic properties.
  • Solvent accessibility is not a strict requirement for residue modification; nearby residues like histidine and tyrosine are enriched near modified sites.

Conclusions:

  • Redox modifications have subtle structural impacts, but can influence protein electrostatics.
  • Specific amino acid motifs surrounding sulfur-containing residues are associated with modification susceptibility.
  • These findings offer potential for predicting redox modification sites on proteins.