The Escherichia coli sensitive to lysis D (SlyD) protein

Function

SlyD 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 Tpeptidyl-prolyl cis–trans isomerase (PPIase) domain and the IF domain, bisected by a deep cleft. The PPIase domain of SlyD possesses a β4–β5a-β5b–α1–β2–β3–α4 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 β6–α3–β9–β8–β7 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