Three-dimensional structure of binase in solution

M. Ya Reibarkh, D. E. Nolde, L. I. Vasilieva, E. V. Bocharov, A. A. Shulga, M. P. Kirpichnikov, A. S. Arseniev

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

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 P-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.

Original languageEnglish
Pages (from-to)250-254
Number of pages5
JournalFEBS Letters
Volume431
Issue number2
DOIs
Publication statusPublished - 17 Jul 1998
Externally publishedYes

Keywords

  • Binase
  • NMR
  • Protection structure
  • Ribonuclease

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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