1T5N
Structural transitions as determinants of calcium-dependent antibiotic daptomycin
Summary for 1T5N
| Entry DOI | 10.2210/pdb1t5n/pdb |
| Related | 1T5M 1XT7 |
| Related PRD ID | PRD_000217 |
| Descriptor | DAPTOMYCIN, DECANOIC ACID (2 entities in total) |
| Functional Keywords | daptomycin, cubicin, antibiotic, lipopeptide, calcium-dependent |
| Biological source | STREPTOMYCES ROSEOSPORUS |
| Total number of polymer chains | 1 |
| Total formula weight | 1656.70 |
| Authors | Jung, D.,Rozek, A.,Okon, M.,Hancock, R.E. (deposition date: 2004-05-04, release date: 2004-08-31, Last modification date: 2019-11-06) |
| Primary citation | Jung, D.,Rozek, A.,Okon, M.,Hancock, R.E. Structural Transitions as Determinants of the Action of the Calcium-Dependent Antibiotic Daptomycin. Chem.Biol., 11:949-, 2004 Cited by PubMed Abstract: 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+). Circular dichroism spectroscopy indicated that daptomycin experienced two structural transitions: a transition upon interaction of daptomycin with Ca2+, and a further transition upon interaction with Ca2+ and the bacterial acidic phospholipid, phosphatidyl glycerol. The Ca2+-dependent insertion of daptomycin into model membranes promoted mild and more pronounced perturbations as assessed by the increase of lipid flip-flop and membrane leakage, respectively. The NMR structure of daptomycin indicated that Ca2+ induced a conformational change in daptomycin that increased its amphipathicity. These results are consistent with the hypothesis that the association of Ca2+ with daptomycin permits it to interact with bacterial membranes with effects that are similar to those of the cationic antimicrobial peptides. PubMed: 15271353DOI: 10.1016/J.CHEMBIOL.2004.04.020 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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