title: The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism.
abstract: We determined the three-dimensional structure of a complex between an archaeal nicotianamine synthase homologue and a chemically synthesised reaction intermediate. This structure suggests that the enzymes cavity allows both an ordered substrate binding and provides energetic coupling of the reaction intermediate formation and translocation.
authors.affiliation: Laboratoire de Bioénergétique Cellulaire - Institut de Biologie Environnementale et Biotechnologie, Commissariat à l'Energie Atomique-UMR 6191 Biologie Végétale et Microbiologie Environnementale, Centre National de la Recherche Scientifique, 13115 Saint-Paul-lez-Durance, France.
authors.forename: Cyril
authors.initials: C
authors.lastname: Dreyfus
authors.forename: Manuel
authors.initials: M
authors.lastname: Larrouy
authors.forename: Florine
authors.initials: F
authors.lastname: Cavelier
authors.forename: Jean
authors.initials: J
authors.lastname: Martinez
authors.forename: David
authors.initials: D
authors.lastname: Pignol
authors.forename: Pascal
authors.initials: P
authors.lastname: Arnoux
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry*; D001665:Binding Sites; D055162:Biocatalysis; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D017013:Methanobacteriaceae / Q000201:enzymology; D017434:Protein Structure, Tertiary
chemical_list: D019843:Archaeal Proteins; D019883:Alkyl and Aryl Transferases; C118230:nicotianamine synthase