MYP_044207
Basic Information
Capistruin
Antimicrobial
Antimicrobial Antibacterial
Antimicrobial Antibacterial Anti-Gram-negative
Standard
19 amino acids
C93H139N27O27
Standard
Sequence
GTPGFQTPDARVISRFGFN
Physicochemical Analysis
2067.26 Da
9.60
0.76
0.56
0.0401
-0.38
0.60
0.02
11.17
41.05
0.1579
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
877.51
-10.62
30.0
28.0
62.0
147.0
5.0
20.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0053221 VERIFIED: YES
Provenance & Taxonomy
Burkholderia thailandensis [Bacterium]; Bacteria [Bacterium]
2; 2
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
RECORD: Rec_0064599 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Anti-Gram-negative
Escherichia coli TOP10
Mex pooled growth assay (OD_ID at 4.5 h; Wald adjusted p-value)
RECORD: Rec_0135312 VERIFIED: YES
Provenance & Taxonomy
Burkholderia thailandensis [Bacterium]
Microcin
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Discovered by genome mining based on the known MccJ25-gene coding cluster McjABCD. Capistruin is endoded by the capABCD gene cluster, where capA encodes the precursor polypeptide, capB cleaves the presursor and is likely to promote the cyclization, capC encodes an enzyme that activates the side chain of Asp9 for cyclization, and capD encodes a immunity protein. Showed activity against closely related Burkholderia and Pseudomonas strains. Chemical modification: Different from the lasso structure of MccJ25, where the N-terminal Gly forms an amide bond with the carboxyl group of Glu8, capistruin forms a 9-residue macrolactam ring formed between NH of Gly1 and the carboxylic side chain of Asp9. Structure: In addition, Arg15 is reponsible for the trapping of the tail in the ring structure. The structure of the peptide in complex with the RNA polymerase (RNAP) has been solved by X-ray crystallography. MOA:bacteria: Like MccJ25, Cap binds within the RNAP secondary channel, not identical to that of MccJ25. Cap binds further from the RNAP active site and does not sterically interfere with NTP binding, and we show that Cap inhibition is partially noncompetitive with respect to NTPs (Braffman et al., 2019). You can rotate, zoom, and view the 3D structure here in the PDB. Recombinant production:bacteria:Burkholderia sp. FERM BP-3421: FERM BP-3421 is a nonpathogenic isolate previously used to produce natural products at industrial scales. In this bacterium, the expression yield is 580-fold higher than that in Escherichia coli. Updated Jan2019; 12/2023; Jan2024
Bio-Activity Profile
Antimicrobial
RECORD: Rec_0167825 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 0.0%, E 10.5%, T 52.6%, C 36.8% [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antibacterial Antimicrobial Anti-Gram-negative
RECORD: Rec_0245350 VERIFIED: YES
Provenance & Taxonomy
Burkholderia thailandensis [Bacterium]
Bacteriocin
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial
Burkholderia and Pseudomonas strains
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