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

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 negat...

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Published in:Applied microbiology and biotechnology 2009-02, Vol.82 (2), p.271-278
Main Authors: Dent, Kyle C, Weber, Brandon W, Benedik, Michael J, Sewell, B. Trevor
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description 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.
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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.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>18946669</pmid><doi>10.1007/s00253-008-1735-4</doi><tpages>8</tpages></addata></record>
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subjects 3d protein reconstruction
Amino Acid Sequence
Amino acids
Ammonia
Biological and medical sciences
Bioremediation
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Chromatography
Cyanide
Cyanide hydratase
Cyanides
Enzymes
Escherichia coli - genetics
Escherichia coli - metabolism
Fibers
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - isolation & purification
Fungal Proteins - metabolism
Fungi
Gene Expression
Hydro-Lyases - chemistry
Hydro-Lyases - genetics
Hydro-Lyases - isolation & purification
Hydro-Lyases - metabolism
Life Sciences
Microbial Genetics and Genomics
Microbiology
Models, Molecular
Molecular Conformation
Molecular Sequence Data
Neurospora crassa
Neurospora crassa - chemistry
Neurospora crassa - enzymology
Nitrilase
Proteins
Sequence Alignment
Studies
title cyanide hydratase from Neurospora crassa forms a helix which has a dimeric repeat
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