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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 |
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creator | Dent, Kyle C Weber, Brandon W Benedik, Michael J Sewell, B. Trevor |
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. |
doi_str_mv | 10.1007/s00253-008-1735-4 |
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Trevor</creator><creatorcontrib>Dent, Kyle C ; Weber, Brandon W ; Benedik, Michael J ; Sewell, B. Trevor</creatorcontrib><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.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-008-1735-4</identifier><identifier>PMID: 18946669</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>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</subject><ispartof>Applied microbiology and biotechnology, 2009-02, Vol.82 (2), p.271-278</ispartof><rights>Springer-Verlag 2008</rights><rights>2009 INIST-CNRS</rights><rights>Springer-Verlag 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-fd00a20f0a336b3cb2ab71d01735184533fa33510fff63c0610c54d46fe03e393</citedby><cites>FETCH-LOGICAL-c454t-fd00a20f0a336b3cb2ab71d01735184533fa33510fff63c0610c54d46fe03e393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/229676343/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/229676343?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,11688,27924,27925,36060,36061,44363,74895</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21096355$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18946669$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dent, Kyle C</creatorcontrib><creatorcontrib>Weber, Brandon W</creatorcontrib><creatorcontrib>Benedik, Michael J</creatorcontrib><creatorcontrib>Sewell, B. Trevor</creatorcontrib><title>cyanide hydratase from Neurospora crassa forms a helix which has a dimeric repeat</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><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.</description><subject>3d protein reconstruction</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Ammonia</subject><subject>Biological and medical sciences</subject><subject>Bioremediation</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Chromatography</subject><subject>Cyanide</subject><subject>Cyanide hydratase</subject><subject>Cyanides</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Fibers</subject><subject>Fundamental and applied biological sciences. 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Trevor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cyanide hydratase from Neurospora crassa forms a helix which has a dimeric repeat</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2009-02-01</date><risdate>2009</risdate><volume>82</volume><issue>2</issue><spage>271</spage><epage>278</epage><pages>271-278</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><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.</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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