3IQD

Structure of Octopine-dehydrogenase in complex with NADH and Agmatine

3IQD の概要

• エントリーDOI: 10.2210/pdb3iqd/pdb
• 関連するPDBエントリー: 3C7A 3C7C 3C7D
• 分子名称: Octopine dehydrogenase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, AGMATINE (3 entities in total)
• 機能のキーワード: octopine, dehydrogenase, oxidoreductase
• 由来する生物種: Pecten maximus (King scallop)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44882.99

構造登録者

Smits, S.H.J.,Meyer, T.,Mueller, A.,Willbold, D.,Grieshaber, M.K.,Schmitt, L. (登録日: 2009-08-20, 公開日: 2010-08-25, 最終更新日: 2023-11-01)

主引用文献

Smits, S.H.J.,Meyer, T.,Mueller, A.,van Os, N.,Stoldt, M.,Willbold, D.,Schmitt, L.,Grieshaber, M.K.
Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography
Plos One, 5:e12312-e12312, 2010

PubMed 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.

PubMed: 20808820
DOI: 10.1371/journal.pone.0012312

実験手法

X-RAY DIFFRACTION (2.8 Å)