title: 1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima.
abstract: HisF comprises one half of the heterodimeric protein complex imidazole glycerol phosphate (IGP) synthase responsible for the fifth step of histidine biosynthesis. Here we report backbone and side chain assignments necessary for characterization of protein dynamics involved in the allosteric mechanism of IGP synthase.
authors.affiliation: Department of Chemistry, Yale University, Sterling Chemistry Laboratory, New Haven, CT, 06511, USA.
authors.forename: James M
authors.initials: JM
authors.lastname: Lipchock
authors.forename: J Patrick
authors.initials: JP
authors.lastname: Loria
mesh_terms: D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons; D020124:Thermotoga maritima / Q000201:enzymology*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; C087227:imidazole glycerol phosphate synthase; D000619:Aminohydrolases