The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism

Chem Commun (Camb). 2011 May 28;47(20):5825-7. doi: 10.1039/c1cc10565e. Epub 2011 Apr 12.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkyl and Aryl Transferases / chemistry*
  • Alkyl and Aryl Transferases / metabolism
  • Archaeal Proteins / chemistry*
  • Binding Sites
  • Biocatalysis
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Methanobacteriaceae / enzymology
  • Protein Structure, Tertiary

Substances

  • Archaeal Proteins
  • Alkyl and Aryl Transferases
  • nicotianamine synthase

Associated data

  • PDB/3O31