General Information
-
DRAMP ID
- DRAMP02901
-
Peptide Name
- Tricyclic peptide MS-271
-
Source
- Streptomyces sp.
-
Family
- Not found
-
Gene
- Not found
-
Sequence
- CLGVGSCNNFAGCGYAIVCFW
-
Sequence Length
- 21
-
UniProt Entry
- P85078
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+
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Target Organism
-
- Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus, Enterococcus faecium.
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
-
Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
-
N-terminal Modification
- Not included yet
-
C-terminal Modification
- Not included yet
-
Nonterminal Modifications and Unusual Amino Acids
- Not included yet
-
Stereochemistry
- Not included yet
-
Structure
- Not found
-
Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- There is no predicted structure for DRAMP02901.
Physicochemical Information
-
Formula
- C97H138N24O26S4
Absent Amino Acids
- DEHKMPQRT
Common Amino Acids
- CG
Mass
- 2184.55
PI
- 5.5
Basic Residues
- 0
Acidic Residues
- 0
Hydrophobic Residues
- 9
Net Charge
- 0
-
Boman Index
- 21.89
Hydrophobicity
- 1.157
Aliphatic Index
- 74.29
Half Life
-
- Mammalian:1.2 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 7240
Absorbance 280nm
- 362
Polar Residues
- 12
DRAMP02901

Comments Information
Function
- Inhibits chicken myosin light chain kinase with an IC50 of 8 M. Antibacterial activity against the Gram-positive bacteria. No antibacterial activity against the Gram-negative bacteria E. coli, K. pneumoniae, P. aeruginosa, P. vulgaris, S. sonnei and S. typhosa. No antifungal activity against C. albicans.
Caution
- The isopeptide linked residue 9 is shown as Asn rather than Asp as mentioned in Ref.1, because it is not known whether Asp or Asn is encoded and the isopeptide bonds are almost always formed between the amides Asn or Gln and N6-lysine or alpha amino groups, with the liberation of an ammonia that makes the reaction essentially irreversible.
PTM
- Contains two disulfide bonds and D-amino acid at position 21.
Literature Information
- ·Literature 1
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Title
- MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.--I. Isolation, structural determination and biological properties of MS-271.
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Pubmed ID
- 8689231
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Reference
- Bioorg Med Chem. 1996 Jan;4(1):115-120.
-
Author
- Yano K, Toki S, Nakanishi S, Ochiai K, Ando K, Yoshida M, Matsuda Y, Yamasaki M.