- Protein Classification
- Protein Links
| 1pxq » Subtilosin A | |
|---|---|
| Hydrophobic Thickness or Depth | 7.6 ± 0.8 Å |
| Tilt Angle | 86 ± 3° |
| ΔGtransfer | -9.3 kcal/mol |
| Links to 1pxq | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | NMR |
| Other PDB entries of this protein | none |
| Number of subunits | 1 |
| Experimental Verification for 1pxq » Subtilosin A |
|---|
| Results are consistent with the partially buried location of subtilosin A in lipid bilayers parallel to the membrane surface, and Trp34 facing towards the center of the lipid bilayer (Thennarasu et al. 2005). |
| 1 reference |
|---|
| Thennarasu S, Lee DK, Poon A, Kawulka KE, Vederas JC, Ramamoorthy A. 2005. Membrane permeabilization, orientation, and antimicrobial mechanism of subtilosin A. Chem. Phys. Lipids. 137:38-51. PubMed |
| Comments on 1pxq » Subtilosin A |
|---|
| This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids. |
