Applied Microbiology and Biotechnology

, Volume 82, Issue 2, pp 271–278

The cyanide hydratase from Neurospora crassa forms a helix which has a dimeric repeat

  • Kyle C. Dent
  • Brandon W. Weber
  • Michael J. Benedik
  • B. Trevor Sewell
Biotechnologically Relevant Enzymes and Proteins

Abstract

The fungal cyanide hydratases form a functionally specialized subset of the nitrilases which catalyze the hydrolysis of cyanide to formamide with high specificity. These hold great promise for the bioremediation of cyanide wastes. The low resolution (3.0 nm) three-dimensional reconstruction of negatively stained recombinant cyanide hydratase fibers from the saprophytic fungus Neurospora crassa by iterative helical real space reconstruction reveals that enzyme fibers display left-handed D1 S5.4 symmetry with a helical rise of 1.36 nm. This arrangement differs from previously characterized microbial nitrilases which demonstrate a structure built along similar principles but with a reduced helical twist. The cyanide hydratase assembly is stabilized by two dyadic interactions between dimers across the one-start helical groove. Docking of a homology-derived atomic model into the experimentally determined negative stain envelope suggests the location of charged residues which may form salt bridges and stabilize the helix.

Keywords

Cyanide Nitrilase 3d protein reconstruction Cyanide hydratase 

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Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • Kyle C. Dent
    • 1
  • Brandon W. Weber
    • 2
  • Michael J. Benedik
    • 3
  • B. Trevor Sewell
    • 2
  1. 1.Department of Molecular and Cell BiologyUniversity of Cape TownRondeboschSouth Africa
  2. 2.Electron Microscope UnitUniversity of Cape TownRondeboschSouth Africa
  3. 3.Department of BiologyTexas A&M UniversityCollege StationUSA

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