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Conserved Residues Lys⁵⁷ and Lys⁴⁰¹ of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.

ABSTRACT: Despite its study since the 1960's, very little is known about the post-translational regulation of the multiple catalytic activities performed by protein disulfide isomerase (PDI), the primary protein folding catalyst of the cell. This work identifies a functional role for the highly conserved CxxC-flanking residues Lys⁵⁷ and Lys⁴⁰¹ of human PDI in vitro. Mutagenesis studies have revealed these residues as modulating the oxidoreductase activity of PDI in a pH-dependent manner. Non-conservative amino acid substitutions resulted in enzyme variants upwards of 7-fold less efficient. This attenuated activity was found to translate into a 2-fold reduction of the rate of electron shuttling between PDI and the intraluminal endoplasmic reticulum oxidase, ERO1α, suggest

SUBMITTER: Caba C

PROVIDER: S-EPMC5835755 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Conserved Residues Lys⁵⁷ and Lys⁴⁰¹ of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.

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Conserved Residues Lys57 and Lys401 of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Conserved Residues Lys⁵⁷ and Lys⁴⁰¹ of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.