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1p0k

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{{STRUCTURE_1p0k| PDB=1p0k | SCENE= }}
{{STRUCTURE_1p0k| PDB=1p0k | SCENE= }}
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'''IPP:DMAPP isomerase type II apo structure'''
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===IPP:DMAPP isomerase type II apo structure===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12798687}}
==About this Structure==
==About this Structure==
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[[Category: Isopentenyl diphosphate]]
[[Category: Isopentenyl diphosphate]]
[[Category: Terpene biosynthesis]]
[[Category: Terpene biosynthesis]]
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Revision as of 06:03, 28 July 2008

Image:1p0k.png

Template:STRUCTURE 1p0k

IPP:DMAPP isomerase type II apo structure

Template:ABSTRACT PUBMED 12798687

About this Structure

1P0K is a Single protein structure of sequence from Bacillus subtilis. 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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