| http://purl.uniprot.org/citations/25596185 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25596185 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25596185 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/25596185 | http://www.w3.org/2000/01/rdf-schema#comment | "The ethylmalonic encephalopathy protein 1 (ETHE1) catalyses the oxygen-dependent oxidation of glutathione persulfide (GSSH) to give persulfite and glutathione. Mutations to the hETHE1 gene compromise sulfide metabolism leading to the genetic disease ethylmalonic encephalopathy. hETHE1 is a mono-iron binding member of the metallo-β-lactamase (MBL) fold superfamily. We report crystallographic analysis of hETHE1 in complex with iron to 2.6 Å resolution. hETHE1 contains an αββα MBL-fold, which supports metal-binding by the side chains of an aspartate and two histidine residues; three water molecules complete octahedral coordination of the iron. The iron binding hETHE1 enzyme is related to the 'classical' di-zinc binding MBL hydrolases involved in antibiotic resistance, but has distinctive features. The histidine and aspartate residues involved in iron-binding in ETHE1, occupy similar positions to those observed across both the zinc 1 and zinc 2 binding sites in classical MBLs. The active site of hETHE1 is very similar to an ETHE1-like enzyme from Arabidopsis thaliana (60% sequence identity). A channel leading to the active site is sufficiently large to accommodate a GSSH substrate. Some of the observed hETHE1 clinical mutations cluster in the active site region. The structure will serve as a basis for detailed functional and mechanistic studies on ETHE1 and will be useful in the development of selective MBL inhibitors."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.org/dc/terms/identifier | "doi:10.1093/hmg/ddv007"xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.org/dc/terms/identifier | "doi:10.1093/hmg/ddv007"xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "Brem J."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "Brem J."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "McDonough M.A."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "McDonough M.A."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "Pettinati I."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/author | "Pettinati I."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/name | "Hum. Mol. Genet."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/name | "Hum. Mol. Genet."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/pages | "2458-2469"xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/pages | "2458-2469"xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/title | "Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/title | "Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy."xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/volume | "24"xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://purl.uniprot.org/core/volume | "24"xsd:string |
| http://purl.uniprot.org/citations/25596185 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25596185 |