This is a default text for your page The Escherichia coli sensitive to lysis D (SlyD) protein. Click above on edit this page to modify. Be careful with the < and > signs.
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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[3].
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[4].
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Disease
Relevance
