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http://purl.uniprot.org/citations/20383014http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20383014http://www.w3.org/2000/01/rdf-schema#comment"Acyl-CoA dehydrogenase [acyl-CoA:(acceptor) 2,3-oxidoreductase; EC 1.3.99.3] catalyzes the first reaction step in mitochondrial fatty-acid beta-oxidation. Here, the very-long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans (cVLCAD) has been cloned and overexpressed in Escherichia coli strain BL21 (DE3). Interestingly, unlike other very-long-chain acyl-CoA dehydrogenases, cVLCAD was found to form a tetramer by size-exclusion chromatography coupled with in-line static light-scattering, refractive-index and ultraviolet measurements. Purified cVLCAD (12 mg ml(-1)) was successfully crystallized by the hanging-drop vapour-diffusion method under conditions containing 100 mM Tris-HCl pH 8.0, 150 mM sodium chloride, 200 mM magnesium formate and 13% PEG 3350. The crystal has a tetragonal form and a complete diffraction data set was collected and processed to 1.8 A resolution. The crystal belonged to space group C2, with unit-cell parameters a = 138.6, b = 116.7, c = 115.3 A, alpha = gamma = 90.0, beta = 124.0 degrees . A self-rotation function indicated the existence of one noncrystallographic twofold axis. A preliminary molecular-replacement solution further confirmed the presence of two molecules in one asymmetric unit, which yields a Matthews coefficient V(M) of 2.76 A(3) Da(-1) and a solvent content of 55%."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.org/dc/terms/identifier"doi:10.1107/s1744309110005002"xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/author"Geng Y."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/author"Fang J."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/author"Li Z."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/author"Sun F."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/author"Zhou Q."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/author"Zhai Y."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/name"Acta Crystallogr Sect F Struct Biol Cryst Commun"xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/pages"426-430"xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/title"Purification, crystallization and preliminary crystallographic analysis of very-long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/20383014http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/20383014http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20383014
http://purl.uniprot.org/citations/20383014http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20383014
http://purl.uniprot.org/uniprot/#_Q19057-mappedCitation-20383014http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20383014
http://purl.uniprot.org/uniprot/#_Q9XWZ2-mappedCitation-20383014http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20383014
http://purl.uniprot.org/uniprot/Q19057http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20383014
http://purl.uniprot.org/uniprot/Q9XWZ2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20383014