2o05

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Revision as of 20:58, 12 November 2007

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spinqualitylabelsall models 2o05, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Human spermidine synthase

Overview

Aminopropyltransferases transfer aminopropyl groups from decarboxylated, S-adenosylmethionine to amine acceptors, forming polyamines. Structural, and biochemical studies have been carried out with the human spermidine, synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine, but is more tolerant of other substrates. Comparison of the structures of, the human spermidine synthase with both substrates and products with the, known structure of T. maritima spermidine synthase complexed to a, multisubstrate analogue inhibitor and analysis of the properties of, site-directed mutants provide a general mechanistic hypothesis for the, aminopropyl transfer reaction. The studies also provide a structural basis, for the specificity of the spermidine synthase subclass of the, aminopropyltransferase family.

About this Structure

2O05 is a Single protein structure of sequence from Homo sapiens with MTA as ligand. This structure superseeds the now removed PDB entry 1ZDZ. Active as Spermidine synthase, with EC number 2.5.1.16 Full crystallographic information is available from OCA.

Reference

Structure and mechanism of spermidine synthases., Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN, Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:17585781

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