1p0n

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[[Image:1p0n.jpg|left|200px]]
[[Image:1p0n.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1p0n |SIZE=350|CAPTION= <scene name='initialview01'>1p0n</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1p0n", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1p0n| PDB=1p0n | SCENE= }}
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|RELATEDENTRY=[[1p0k|1P0K]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0n OCA], [http://www.ebi.ac.uk/pdbsum/1p0n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p0n RCSB]</span>
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}}
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'''IPP:DMAPP isomerase type II, FMN complex'''
'''IPP:DMAPP isomerase type II, FMN complex'''
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[[Category: Rohdich, F.]]
[[Category: Rohdich, F.]]
[[Category: Steinbacher, S.]]
[[Category: Steinbacher, S.]]
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[[Category: dimethylallyl diphosphate]]
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[[Category: Dimethylallyl diphosphate]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: isomerase]]
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[[Category: Isomerase]]
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[[Category: isopentenyl diphosphate]]
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[[Category: Isopentenyl diphosphate]]
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[[Category: terpene biosynthesis]]
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[[Category: Terpene biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:32:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:53:10 2008''
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Revision as of 01:32, 3 May 2008

Image:1p0n.jpg

Template:STRUCTURE 1p0n

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. 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 Page seeded by OCA on Sat May 3 04:32:01 2008

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