1dxl

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spinqualitylabelsall models 1dxl, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

DIHYDROLIPOAMIDE DEHYDROGENASE OF GLYCINE DECARBOXYLASE FROM PISUM SATIVUM

Overview

The glycine decarboxylase complex consists of four different component, enzymes (P-, H-, T- and L-proteins). The 14-kDa lipoamide-containing, H-protein plays a pivotal role in the complete sequence of reactions as, its prosthetic group (lipoic acid) interacts successively with the three, other components of the complex and undergoes a cycle of reductive, methylamination, methylamine transfer and electron transfer. With the aim, to understand the interaction between the H-protein and its different, partners, we have previously determined the crystal structure of the, oxidized and methylaminated forms of the H-protein. In the present study, we have crystallized the H-protein in its reduced state and the L-protein, (lipoamide dehydrogenase or dihydrolipoamide dehydrogenase). The L-protein, ... [(full description)]

About this Structure

1DXL is a [Single protein] structure of sequence from [Pisum sativum] with FAD as [ligand]. Active as [Dihydrolipoyl dehydrogenase], with EC number [1.8.1.4]. Structure known Active Sites: FAA, FAB, FAC and FAD. Full crystallographic information is available from [OCA].

Reference

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins., Faure M, Bourguignon J, Neuburger M, MacHerel D, Sieker L, Ober R, Kahn R, Cohen-Addad C, Douce R, Eur J Biochem. 2000 May;267(10):2890-8. PMID:10806386

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