1t5n

Structural transitions as determinants of calcium-dependent antibiotic daptomycin

spinqualitylabelsall models 1t5n Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1t5n is a 1 chain structure with sequence from Streptomyces filamentosus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 17 models Ligands: DAL, DKA, DSG, DSN, KYN, LME, ORN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin.,Jung D, Rozek A, Okon M, Hancock RE Chem Biol. 2004 Jul;11(7):949-57. PMID:15271353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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