Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD

Table 1 Peptides used in this study

Name	Sequence	Charge	Source
Name	Sequence	Charge	UniProt	Position
S2	TRYWNPKMKPFIFGA	+3	P0A7V0	20–34
S2-minus1	GHQTRYWNPKMKPFI	+3 to +4		17–31
S2-minus2	VHFGHQTRYWNPKMK	+3 to +5		14–28
S2-minus3	KAGVHFGHQTRYWNP	+2 to +4		11–25
S2-plus1	WNPKMKPFIFGARNK	+4		23–37
S2-plus2	KMKPFIFGARNKVHI	+4 to +5		26–40
S2-long2	QTRYWNPKMKPFIFGAR	+4		19–35
S2-long4	HQTRYWNPKMKPFIFGARN	+4 to +5		18–36
S2-long6	GHQTRYWNPKMKPFIFGARNK	+5 to +6		17–37
S2-long8	FGHQTRYWNPKMKPFIFGARNKV	+5 to +6		16–38
S2-short2	RYWNPKMKPFIFG	+3		21–33
S2-short4	YWNPKMKPFIF	+2		22–32
S2-short6	WNPKMKPFI	+2		23–31
S2-short8	WNPKMKP	+2		23–29
S3	RLGIVKPWNSTWFAN	+2	P0A7V3	11–25
T1	VGSNSYPHKYNNYEG	0 to +1	P00651	59–73
SlpA linker	SGLVPRGS	+1	-	-

For peptides derived from the S2 protein, parts overlapping the original S2 peptide are underlined. The expected charges at neutral pH are listed. These were calculated using −1 for Glu and Asp, +1 for Lys and Arg, and 0 or +1 for His (for peptides with His residues, the charge is given as a range). In addition to the peptides listed here, we also used the following five mutants of the S2 peptide: P25A, P29E, P25A/P29E, P25N/P29N, and W23A

ISSN: 1741-7007