- Protein Classification
- Protein Links
| 1t5m » Daptomycin, Ca-free | |
|---|---|
| Hydrophobic Thickness or Depth | 2.3 ± 1.3 Å |
| Tilt Angle | 33 ± 6° |
| ΔGtransfer | -7.9 kcal/mol |
| Links to 1t5m | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | NMR |
| Other PDB entries of this protein | 1t5n, 1xt7 |
| Number of subunits | 1 |
| Experimental Verification for 1t5m » Daptomycin, Ca-free |
|---|
| Kyn14 residue is situated at the lipid-water interface and penetrates deeper into the membrane in the Ca-bound state (Lakey and Ptak 1988). |
| 3 references |
|---|
| Baltz RH, Miao V, Wrigley SK. 2005. Natural products to drugs: daptomycin and related lipopeptide antibiotics. Nat Prod Rep. 22:717-41. PubMed |
| Jung D, Rozek A, Okon M, Hancock RE. 2004. Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin. Chem Biol. 11:949-57. PubMed |
| Lakey JH, Ptak M. 1988. Fluorescence indicates a calcium-dependent interaction between the lipopeptide antibiotic LY146032 and phospholipid membranes. Biochemistry. 27:4639-4. PubMed |
| Comments on 1t5m » Daptomycin, Ca-free |
|---|
| Daptomycin is a cyclic anionic lipopeptide antibiotic recently approved for the treatment of complicated skin infections (Cubicin). Its function is dependent on calcium (as Ca2+). The NMR structure of daptomycin indicated that Ca2+ induced a conformational change in daptomycin that increased its amphipathicity (Jung et al. 2004). |
