From the Producer Microorganisms to the Lasso Scaffold - Lasso Peptides: Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds - page 20

Table 2.5 (continued)

Peptide Peptide

length (aa)

Peptide net
charge a

Method for
analysis of 3D
structure

Ring size
(aa (Nb of
atoms))

Ring forming
residue

Lasso stabilization
plugs b

C-terminal
tail
size (aa)

References

Syanodin I d 21/17 3−/1− N.E./Char 8 (25) Asp8 n.i. 9 (Hegemann et al. 2013b )

Xanthomonin I e
Xanthomonin II e
Xanthomonin III e

20/16
20/14
20/13 a

4−/2−
3−/2−
3−/1−

X-ray
NMR

7 (23)
7(23)
7 (23)

Glu7
Glu7
Glu7

Ile9/ Phe12
Met9/ Ile12
Met11

13/9
13/7
13/6

(Hegemann et al. 2014 )

Zucinodin 16 3− N.E./Char 8 (26) Glu8 n.d. n.i. 8 (Hegemann et al. 2013b )
N.E./Char. 3D structure not established by NMR or X-ray crystallography, but characteristics of the lasso topology demonstrated by MS and/or NMR and/or
biochemical methods (carboxypeptidase Y assay and/or variant production in particular)
N.E. 3D structure not established; potential lasso peptide .
n.i. not identified
a Histidine has been considered as positively charged
b The plug residue below the ring is in bold character whereas the upper plug is not. Plugs that have been hypothesized but not identified by structural analysis
or mutagenesis are in italics
c Lariatin A is the 18 amino acid form of lariatin B (now termed lariatin) truncated at the C-terminus; propeptin-2 is the 17 amino acid form of propeptin trun-
cated at the C-terminus
d Astexin 1 was produced from the wild type strain and by heterologous expression under a 23-amino acid form accompanied by truncated forms, among which
astexin 1(19) was characterized; caulododins I, II, III differ by several amino acid substitutions in both the ring and tail, but not in sizes of the ring and tail;
all three peptides have been isolated under 17-amino acid C-terminal truncated forms; sphingonodins I and II are 17- and 19- amino acid C-terminal truncated
forms; rhodanodin is the 17 amino acid C-terminal truncated form; sphyngopixins I and II are 19- and 21- amino acid C-terminal truncated forms; syanodin I is
the 17- amino acid C-terminal truncated form. The number of residues of both the full length and truncated forms is indicated
e Xanthomonins I, II, III were obtained upon production optimization in truncated forms lacking 4, 6 and 7 amino acids at the C-terminus, respectively; the size
of both the full length and main truncated peptides is mentioned in the table