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| | <StructureSection load='2vnq' size='340' side='right'caption='[[2vnq]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2vnq' size='340' side='right'caption='[[2vnq]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vnq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecobb Ecobb]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2vej 2vej]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VNQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vnq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2vej 2vej]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VNQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nfs|1nfs]], [[1q54|1q54]], [[1ppv|1ppv]], [[1ow2|1ow2]], [[1ppw|1ppw]], [[1x84|1x84]], [[1i9a|1i9a]], [[1nfz|1nfz]], [[1r67|1r67]], [[1x83|1x83]], [[1hx3|1hx3]], [[1hzt|1hzt]], [[1pvf|1pvf]], [[2vnp|2vnp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vnq OCA], [https://pdbe.org/2vnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vnq RCSB], [https://www.ebi.ac.uk/pdbsum/2vnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vnq ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vnq OCA], [https://pdbe.org/2vnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vnq RCSB], [https://www.ebi.ac.uk/pdbsum/2vnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vnq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/IDI_ECOLI IDI_ECOLI]] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).<ref>PMID:10099534</ref> <ref>PMID:9603997</ref>
| + | [https://www.uniprot.org/uniprot/IDI_ECOLI IDI_ECOLI] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).<ref>PMID:10099534</ref> <ref>PMID:9603997</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecobb]] | + | [[Category: Escherichia coli BL21]] |
| - | [[Category: Isopentenyl-diphosphate Delta-isomerase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oudjama, Y]] | + | [[Category: Oudjama Y]] |
| - | [[Category: Ruyck, J de]] | + | [[Category: Wouters J]] |
| - | [[Category: Wouters, J]] | + | [[Category: De Ruyck J]] |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Ipp isomerase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Isoprene biosynthesis]]
| + | |
| - | [[Category: Magnesium]]
| + | |
| - | [[Category: Manganese]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| Structural highlights
Function
IDI_ECOLI Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Type 1 isopentenyl diphosphate isomerase (IDI-1) has been crystallized in a new crystal form. After data collection from small thin needle-shaped crystals, a new monoclinic form of the studied protein was identified. In this article, the three crystal forms of IDI-1 (orthorhombic, monoclinic and trigonal) are compared.
Monoclinic form of isopentenyl diphosphate isomerase: a case of polymorphism in biomolecular crystals.,de Ruyck J, Oudjama Y, Wouters J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):239-42. Epub 2008 Mar 21. PMID:18391416[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang CW, Oh MK, Liao JC. Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli. Biotechnol Bioeng. 1999 Jan 20;62(2):235-41. PMID:10099534
- ↑ Hemmi H, Ohnuma S, Nagaoka K, Nishino T. Identification of genes affecting lycopene formation in Escherichia coli transformed with carotenoid biosynthetic genes: candidates for early genes in isoprenoid biosynthesis. J Biochem. 1998 Jun;123(6):1088-96. PMID:9603997
- ↑ de Ruyck J, Oudjama Y, Wouters J. Monoclinic form of isopentenyl diphosphate isomerase: a case of polymorphism in biomolecular crystals. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):239-42. Epub 2008 Mar 21. PMID:18391416 doi:10.1107/S174430910800568X
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