The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanismElectronic supplementary information (ESI) available: Experimental details; a movie of the reaction catalysed by MtNAS. See DOI: 10.1039/c1cc10565e

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. [ABSTRACT FROM AUTHOR]