Issue 20, 2011
From the journal:

Chemical Communications

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

Cyril Dreyfus,a   Manuel Larrouy,b   Florine Cavelier,b   Jean Martinez,b   David Pignola  and  Pascal Arnoux*a  

* Corresponding authors

a 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
E-mail: pascal.arnoux@cea.fr
Fax: +33 44225 4701
Tel: +33 44225 3570

b IBMM, UMR-CNRS 5247, Université Montpellier 1 et 2, 34095 Montpellier, France

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.

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

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Article information

DOI
https://doi.org/10.1039/C1CC10565E
Article type
Communication
Submitted
28 Jan 2011
Accepted
16 Mar 2011
First published
12 Apr 2011

Chem. Commun., 2011,47, 5825-5827

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

C. Dreyfus, M. Larrouy, F. Cavelier, J. Martinez, D. Pignol and P. Arnoux, Chem. Commun., 2011, 47, 5825 DOI: 10.1039/C1CC10565E

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