Antimicrobial Peptide AP02962

     
 

APD ID:

AP02962

 
 

Name/Class:

Tur1A (Dolphin, mammals, animals; Pro-rich; Arg-rich; UCLL1; BBribo)

 
 

Source:

Tursiopt truncatus

 
 

Sequence:

RRIRFRPPYLPRPGRRPRFPPPFPIPRIPRIP

 
 

Length:

32

 
 

Net charge:

10

 
 

Hydrophobic residue%:

25%

 
 

Boman Index:

3.58 kcal/mol

 
 

3D Structure:

Rich

 
 

Method:

X-ray

 
 

SwissProt ID:

PDB ID: 6FKR   Go to PDB

 
 

Activity:

Anti-Gram-,

 
 

Crucial residues:

 
 

Additional info:

APD analysis reveals that the sequence of the peptide shows 57% similarity to PR-39. molecular formula: C188H300N62O34; Mol Wt: 3972.858; GRAVY = -1.11. Active against E. coli BW25113 (MIC 1.2 uM). Peptide truncation indicates that the antimicrobial activity is mainly located at the N-terminal region residues 1-16 (MIC 4 uM). While the intact molecule shows similar activity against sbmA and yjiL KO strains, the truncated peptides 1-16, 8-24, and 16-32 are inactive, indicating the entire sequence do not depend on the Pro-rich peptide transporters for activity. Tur1A inhibits E. coli protein translation by binding to the exit tunnel of ribosome in a reversed order. Interestingly, residues 1-16 plays a major role in ribosome binding. You can rotate, zoom, and view the lipid II bound 3D structure here in the PDB. 3/2018.

 
       
 

Title:

The Dolphin Proline-Rich Antimicrobial Peptide Tur1A Inhibits Protein Synthesis by Targeting the Bacterial Ribosome.

 
 

Author:

Mardirossian M, Pérébaskine N, Benincasa M, Gambato S, Hofmann S, Huter P, Müller C, Hilpert K, Innis CA, Tossi A, Wilson DN.2018

 
 

Reference:

Cell Chem Biol. 2018 May 17;25(5):530-539.e7. doi: 10.1016/j.chembiol.2018.02.004. PubMed

 
       

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