1p0n

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(New page: 200px<br /><applet load="1p0n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p0n, resolution 2.8&Aring;" /> '''IPP:DMAPP isomerase t...)
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[[Image:1p0n.jpg|left|200px]]<br /><applet load="1p0n" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p0n, resolution 2.8&Aring;" />
caption="1p0n, resolution 2.8&Aring;" />
'''IPP:DMAPP isomerase type II, FMN complex'''<br />
'''IPP:DMAPP isomerase type II, FMN complex'''<br />
==Overview==
==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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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==
==About this Structure==
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1P0N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P0N OCA].
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1P0N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0N OCA].
==Reference==
==Reference==
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[[Category: terpene biosynthesis]]
[[Category: terpene biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:21:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:44 2008''

Revision as of 12:23, 21 February 2008

Image:1p0n.jpg

1p0n, resolution 2.8Å

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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 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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