Three‐dimensional structure of binase in solution

FEBS Letters

Kirpichnikov, M.P¹  Reibarkh, M.Ya¹  Nolde, D.E¹  Arseniev, A.S¹  Vasilieva, L.I¹  Bocharov, E.V¹  Shulga, A.A¹ 

[1] Shemyakin - Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow 117871, Russia

关键词: Ribonuclease;    Binase;    NMR;    Protein structure;    NMR;    nuclear magnetic resonance;    2D;    two-dimensional;    NOE;    nuclear Overhauser effect;    DQF-COSY;    2D double quantum filtered correlated spectroscopy;    NOESY;    2D NOE-correlated spectroscopy;    TAD;    torsion angle dynamics;    PDB;    Brookhaven Protein Data Bank;    rmsd;    root mean square deviation;   

DOI  :  10.1016/S0014-5793(98)00765-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We present the spatial structure of binase, a small extracellular ribonuclease, derived from ¹H-NMR* data in aqueous solution. The total of 20 structures were obtained via torsion angle dynamics using DYANA program with experimental NOE and hydrogen bond distance constraints and φ and χ¹ dihedral angle constraints. The final structures were energy minimised with ECEPP/2 potential in FANTOM program. Binase consists of three α-helices in N-terminal part (residues 6–16, 26–32 and 41–44), five-stranded antiparallel β-sheet in C-terminal part (residues 51–55, 70–75, 86–90, 94–99 and 104–108) and two-stranded parallel β-sheet (residues 22–24 and 49–51). Three loops (residues 36–39, 56–67 and 76–83), which play significant role in biological functioning of binase, are flexible in solution. The differences between binase and barnase spatial structures in solution explain the differences in thermostability of binase, barnase and their hybrids.

【 授权许可】

Unknown