Studies on the secondary structure of the peptide antibiotic antiamoebin I.
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Biomedical subjects
Publications and source records attributed to V Pattabhi.
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X-ray crystallographic study of the ferredoxin-like protein (iron-sulfur protein III) from Azotobacter vinelandii has been extended to 2.5-A resolution. A 4.0-A resolution electron density map revealed that the molecule contains two Fe-S clusters of differing size and shape separated by 12 A (Stout, C.D. (1979) Nature 279, 83-84). Recent Mössbauer results by Emptage et al. (Emptage, M.H., Kent, T.A., Huynh, B.H., Rawlings, J., Orme-Johnson, W.H., and Münck, E. (1980) J. Biol. Chem. 255, 1793-1796) have shown that the molecule contains 7 iron atoms as a high potential iron protein-like Fe4 center and a novel 3-Fe center. The 2.5-A electron density map shows two distinctly different Fe-S clusters. The larger cluster consists of a tetranuclear [4Fe-4S] core ligated to the protein at each iron atom. The smaller cluster is distinctly planar and cannot be modeled with [2Fe-2S] or [4Fe-4S] structures. The best model for this cluster is a [3Fe-3S] core. The protein makes six contacts with this cluster.
Cholesteryl decanoate (C37H64O2) is monoclinic, space group P2I, with cell dimensions a = 12.931 (6), b = 9.066 (2), c = 30.22 (1) A, beta = 91.14 (4) degrees, and Z = 4. The atomic coordinates from cholesteryl laurate were used in an initial trial structure which was refined by block diagonal least-squares methods with 1846 observed X-ray reflections (R = 0.129). Molecules A and B have almost fully extended conformations, except at the ester bonds and towards the end of the decanoate B chain. The molecules are arranged in antiparallel array forming monolayers of thickness d001 = 30.22 A, with the molecular long axis making an angle of about 67 degrees with the layer interface. The crystal structure is very similar to that of cholesteryl nonanoate and cholesteryl laurate.