Journal Article

PreJuSER-11495

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography

Smits, S. H. J.FZJ* ; Meyer, T.FZJ* ; Müller, A.FZJ* ; van Os, N.FZJ* ; Stoldt, M.FZJ* ; Willbold, D.FZJ* ; Schmitt, L.FZJ* ; Grieshaber, M. K.FZJ*

2010
PLoS Lawrence, Kan.

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Please use a persistent id in citations: http://hdl.handle.net/2128/11184  doi:10.1371/journal.pone.0012312

Abstract: Octopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to octopine, NAD(+), and water during escape swimming and/or subsequent recovery. The structure of OcDH was recently solved and a reaction mechanism was proposed which implied an ordered binding of NADH, L-arginine and finally pyruvate. Here, the order of substrate binding as well as the underlying conformational changes were investigated by NMR confirming the model derived from the crystal structures. Furthermore, the crystal structure of the OcDH/NADH/agmatine complex was determined which suggests a key role of the side chain of L-arginine in protein cataylsis. Thus, the order of substrate binding to OcDH as well as the molecular signals involved in octopine formation can now be described in molecular detail.

Keyword(s): Agmatine: pharmacology (MeSH) ; Amino Acid Oxidoreductases: antagonists & inhibitors (MeSH) ; Amino Acid Oxidoreductases: chemistry (MeSH) ; Amino Acid Oxidoreductases: metabolism (MeSH) ; Animals (MeSH) ; Crystallography, X-Ray (MeSH) ; Ligands (MeSH) ; Models, Molecular (MeSH) ; Nuclear Magnetic Resonance, Biomolecular (MeSH) ; Pecten: enzymology (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Tertiary (MeSH) ; Ligands ; Agmatine ; Amino Acid Oxidoreductases ; D-octopine dehydrogenase ; J

Note: This work was supported by the Deutsche Forschungs Gemeinschaft (grant GR456/20-4 to M.K.G.) and a stipendium of the North Rhein Westphalia graduate school Biostruct to T.M. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

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Contributing Institute(s):

1. Strukturbiochemie (ISB-3)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2010

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