Role of polar and nonpolar residues at the active site for PPIase activity of FKBP22 fromShewanellasp. SIB1

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Abstract

Database

Peptidyl prolyl cis–trans isomerase (PPIase, EC5.2.1.8)

Database

We show that Asp137, Arg142, Trp157, and Phe197, which are located at the substrate binding cavity of SIB1 FKBP22 from Shewanella sp. SIB1, are important for peptidyl prolyl cis-trans isomerase (PPIase) activity of this protein. We propose the catalytic mechanism of this protein, and we also show that SIB1 FKBP22 does not require PPIase activity for chaperone function.

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