1p0n

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Revision as of 21:13, 20 November 2007

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spinqualitylabelsall models 1p0n, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

IPP:DMAPP isomerase type II, FMN complex

Overview

Two types of isopentenyl diphosphate:dimethylallyl diphosphate isomerases, (IDI) have been characterized at present. The long known IDI-1 is only, dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. Here, we report the first structure of an IDI-2 from, Bacillus subtilis at 1.9A resolution in the ligand-free form and of the, FMN-bound form at 2.8A resolution. The enzyme is an octamer that forms a, D4 symmetrical open, cage-like structure. The monomers of 45 kDa display a, classical TIM barrel fold. FMN is bound only with very moderate affinity, and is therefore completely lost during purification. However, the enzyme, can be reconstituted in the crystals by soaking with FMN. Three, glycine-rich sequence stretches that are characteristic for IDI-2, participate in FMN binding within the interior of the cage. Regions, harboring strictly conserved residues that are implicated in substrate, binding or catalysis remain largely disordered even in the presence of, FMN.

About this Structure

1P0N is a Single protein structure of sequence from Bacillus subtilis with FMN as ligand. Active as Isopentenyl-diphosphate Delta-isomerase, with EC number 5.3.3.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis., Steinbacher S, Kaiser J, Gerhardt S, Eisenreich W, Huber R, Bacher A, Rohdich F, J Mol Biol. 2003 Jun 20;329(5):973-82. PMID:12798687

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