1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

FEBS Letters

Hanzawa, Hiroyuki²  Kohda, Daisuke¹  Komano, Hiroto²  Natori, Shunji²  Shimada, Ichio²  Arata, Yoji²  Inagaki, Fuyuhiko¹  Kuzuhara, Takashi² 

[1] Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Komagome, Tokyo 113, Japan;Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Hongo, Tokyo 113, Japan

关键词: Antibacterial activity;    Cardiolipin;    Dynamical simulated annealing;    Sapecin;    Tertiary structure;    2D NMR;    DANTE;    delays alternating with nutation for tailored excitation;    DQF-COSY;    double quantum filtered correlated spectroscopy;    HOHAHA;    homonuclear Hartmann-Hahn spectroscopy;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    NOESY;    2-dimensional NOE spectroscopy;   

DOI  :  10.1016/0014-5793(90)81206-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The solution conformation of an antibacterial protein sapecin has been determined by ¹H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4–12), one helix (residues 15–23), and two extended strands (residues 24–31 and 34–40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.

【 授权许可】

Unknown