http://purl.uniprot.org/citations/34099860 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/34099860 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/34099860 | http://www.w3.org/2000/01/rdf-schema#comment | "Aconitase superfamily members catalyze the homologous isomerization of specific substrates by sequential dehydration and hydration and contain a [4Fe-4S] cluster. However, monomeric and heterodimeric types of function unknown aconitase X (AcnX) have recently been characterized as a cis-3-hydroxy-L-proline dehydratase (AcnXType-I) and mevalonate 5-phosphate dehydratase (AcnXType-II), respectively. We herein elucidated the crystal structures of AcnXType-I from Agrobacterium tumefaciens (AtAcnX) and AcnXType-II from Thermococcus kodakarensis (TkAcnX) without a ligand and in complex with substrates. AtAcnX and TkAcnX contained the [2Fe-2S] and [3Fe-4S] clusters, respectively, conforming to UV and EPR spectroscopy analyses. The binding sites of the [Fe-S] cluster and substrate were clearlydifferent from those that were completely conserved in other aconitase enzymes; however, theoverall structural frameworks and locations of active sites were partially similar to each other.These results provide novel insights into the evolutionary scenario of the aconitase superfamilybased on the recruitment hypothesis."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.org/dc/terms/identifier | "doi:10.1038/s42003-021-02147-5"xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.org/dc/terms/identifier | "doi:10.1038/s42003-021-02147-5"xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Watanabe Y."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Watanabe Y."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Watanabe S."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Watanabe S."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Murase Y."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Murase Y."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Tajima K."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Tajima K."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Sakurai Y."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/author | "Sakurai Y."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/name | "Commun. Biol."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/name | "Commun Biol"xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/pages | "687"xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/pages | "687"xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/title | "Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/title | "Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily."xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/volume | "4"xsd:string |
http://purl.uniprot.org/citations/34099860 | http://purl.uniprot.org/core/volume | "4"xsd:string |