Literature summary for 2.3.2.23 extracted from

Williams, C.; Van Den Berg, M.; Stanley, W.; Wilmanns, M.; Distel, B.
A disulphide bond in the E2 enzyme Pex4p modulates ubiquitin-conjugating activity (2013), Sci. Rep., 3, 2212.

Search for more literature for 2.3.2.23

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22. Structure shows a narrowing of the active site cleft, caused by loss of the disulfide bond	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
C105S/C146S	mutation of the residues forming an intramolecular disulfide bond. Mutation does not disturb the secondary structure of the protein but does reduce the in vitro activity of isoform Pex4	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P29340	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	isoform Pex4 can form a disulfide bond between the cysteine residues at positions 105 and 146. Mutating the disulfide forming cysteine residues to serines does not disturb the secondary structure of the protein but does reduce the in vitro activity of Pex4. Structure of mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22 shows a narrowing of the active site cleft, caused by loss of the disulfide bond. This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4 activity	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
Pex4	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)