| http://purl.uniprot.org/citations/36197914 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/36197914 | http://www.w3.org/2000/01/rdf-schema#comment | "α-Carboxyketose synthases, including 3-deoxy-d-arabinoheptulosonate 7-phosphate synthase (DAHPS), are long-standing targets for inhibition. They are challenging targets to create tight-binding inhibitors against, and inhibitors often display half-of-sites binding and partial inhibition. Half-of-sites inhibition demonstrates the existence of inter-subunit communication in DAHPS. We used X-ray crystallography and spatially resolved hydrogen-deuterium exchange (HDX) to reveal the structural and dynamic bases for inter-subunit communication in Escherichia coli DAHPS(Phe), the isozyme that is feedback-inhibited by phenylalanine. Crystal structures of this homotetrameric (dimer-of-dimers) enzyme are invariant over 91% of its sequence. Three variable loops make up 8% of the sequence and are all involved in inter-subunit contacts across the tight-dimer interface. The structures have pseudo-twofold symmetry indicative of inter-subunit communication across the loose-dimer interface, with the diagonal subunits B and C always having the same conformation as each other, while subunits A and D are variable. Spatially resolved HDX reveals contrasting responses to ligand binding, which, in turn, affect binding of the second substrate, erythrose-4-phosphate (E4P). The N-terminal peptide, M1-E12, and the active site loop that binds E4P, F95-K105, are key parts of the communication network. Inter-subunit communication appears to have a catalytic role in all α-carboxyketose synthase families and a regulatory role in some members."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.biochem.2c00465"xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Wilson D.J."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Junop M.S."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Balachandran N."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Berti P.J."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Liuni P."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Grainger R.A."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/author | "Rob T."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/pages | "2229-2240"xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/title | "Role of Half-of-Sites Reactivity and Inter-Subunit Communications in DAHP Synthase Catalysis and Regulation."xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://purl.uniprot.org/core/volume | "61"xsd:string |
| http://purl.uniprot.org/citations/36197914 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/36197914 |
| http://purl.uniprot.org/citations/36197914 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/36197914 |
| http://purl.uniprot.org/uniprot/#_P0AB91-mappedCitation-36197914 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/36197914 |
| http://purl.uniprot.org/uniprot/P0AB91 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/36197914 |