| http://purl.uniprot.org/citations/29717994 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29717994 | http://www.w3.org/2000/01/rdf-schema#comment | "Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the three-dimensional crystal structure of GAPDH treated with trehalose is reported at 2.0 Å resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose-bound ecGAPDH was compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure."xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://purl.org/dc/terms/identifier | "doi:10.1107/s2053230x18004557"xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://purl.uniprot.org/core/author | "Kim Y.J."xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29717994 | http://purl.uniprot.org/core/name | "Acta Crystallogr F Struct Biol Commun"xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://purl.uniprot.org/core/pages | "277-282"xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://purl.uniprot.org/core/title | "A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase."xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://purl.uniprot.org/core/volume | "74"xsd:string |
| http://purl.uniprot.org/citations/29717994 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29717994 |
| http://purl.uniprot.org/citations/29717994 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/29717994 |
| http://purl.uniprot.org/uniprot/#_P0A9B2-mappedCitation-29717994 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/29717994 |
| http://purl.uniprot.org/uniprot/P0A9B2 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/29717994 |