1p0k

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[[Image:1p0k.jpg|left|200px]]
 
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{{Structure
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==IPP:DMAPP isomerase type II apo structure==
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|PDB= 1p0k |SIZE=350|CAPTION= <scene name='initialview01'>1p0k</scene>, resolution 1.9&Aring;
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<StructureSection load='1p0k' size='340' side='right'caption='[[1p0k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1p0k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0K FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0k OCA], [https://pdbe.org/1p0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0k RCSB], [https://www.ebi.ac.uk/pdbsum/1p0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0k ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1p0n|1P0N]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0k OCA], [http://www.ebi.ac.uk/pdbsum/1p0k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p0k RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/IDI2_BACSU IDI2_BACSU] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p0k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p0k ConSurf].
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<div style="clear:both"></div>
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'''IPP:DMAPP isomerase type II apo structure'''
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==See Also==
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*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
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__TOC__
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==Overview==
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</StructureSection>
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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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==About this Structure==
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1P0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0K OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12798687 12798687]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Isopentenyl-diphosphate Delta-isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bacher A]]
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[[Category: Bacher, A.]]
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[[Category: Eisenreich W]]
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[[Category: Eisenreich, W.]]
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[[Category: Gerhardt S]]
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[[Category: Gerhardt, S.]]
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[[Category: Huber R]]
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[[Category: Huber, R.]]
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[[Category: Kaiser J]]
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[[Category: Kaiser, J.]]
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[[Category: Rohdich F]]
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[[Category: Rohdich, F.]]
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[[Category: Steinbacher S]]
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[[Category: Steinbacher, S.]]
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[[Category: dimethylallyl diphosphate]]
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[[Category: flavoprotein]]
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[[Category: isomerase]]
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[[Category: isopentenyl diphosphate]]
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[[Category: terpene biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:53:03 2008''
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Current revision

IPP:DMAPP isomerase type II apo structure

PDB ID 1p0k

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