Function
is a member of the FK506-binding protein (FKBP) family, it harbours prolyl isomerase activity, which is responsible for accelerating the rate-limiting trans-to-cis isomerization step in protein folding[1].
Structural highlights
In solution, SlyD folds into two globular domains, namely the and the , bisected by a deep . The PPIase domain of SlyD possesses a topology, and folds to generate a twisted four-stranded antiparallel b-sheet wrapped around the α1-helix and flanked by the α4-helix. The IF domain of SlyD displays a topology, and folds to generate a four-stranded antiparallel b-sheet bordered by a short α3-helix[2].
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Disease
Relevance
3D structures of SlyD
Peptidyl-prolyl cis-trans isomerase
