1woh

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spinqualitylabelsall models 1woh, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

Overview

Agmatine is the product of arginine decarboxylation and can be hydrolyzed, by agmatinase to putrescine, the precursor for biosynthesis of higher, polyamines, spermidine, and spermine. Besides being an intermediate in, polyamine metabolism, recent findings indicate that agmatine may play, important regulatory roles in mammals. Agmatinase is a binuclear manganese, metalloenzyme and belongs to the ureohydrolase superfamily that includes, arginase, formiminoglutamase, and proclavaminate amidinohydrolase., Compared with a wealth of structural information available for arginases, no three-dimensional structure of agmatinase has been reported. Agmatinase, from Deinococcus radiodurans, a 304-residue protein, shows approximately, 33% of sequence identity to human mitochondrial agmatinase. Here we report, the crystal structure of D. radiodurans agmatinase in Mn(2+)-free, Mn(2+)-bound, and Mn(2+)-inhibitor-bound forms, representing the first, structure of agmatinase. It reveals the conservation as well as variation, in folding, oligomerization, and the active site of the ureohydrolase, superfamily. D. radiodurans agmatinase exists as a compact homohexamer of, 32 symmetry. Its binuclear manganese cluster is highly similar but not, identical to the clusters of arginase and proclavaminate amidinohydrolase., The structure of the inhibited complex reveals that inhibition by, 1,6-diaminohexane arises from the displacement of the metal-bridging, water.

About this Structure

1WOH is a Single protein structure of sequence from Deinococcus radiodurans. Active as Agmatinase, with EC number 3.5.3.11 Full crystallographic information is available from OCA.

Reference

Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily., Ahn HJ, Kim KH, Lee J, Ha JY, Lee HH, Kim D, Yoon HJ, Kwon AR, Suh SW, J Biol Chem. 2004 Nov 26;279(48):50505-13. Epub 2004 Sep 7. PMID:15355972

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