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| | <StructureSection load='2ww4' size='340' side='right'caption='[[2ww4]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2ww4' size='340' side='right'caption='[[2ww4]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ww4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ww4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WW4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-(cytidine_5'-diphospho)-2-C-methyl-D-erythritol_kinase 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.148 2.7.1.148] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ww4 OCA], [https://pdbe.org/2ww4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ww4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ww4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ww4 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=2ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ww4 OCA], [https://pdbe.org/2ww4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ww4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ww4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ww4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ISPE_ECO8A ISPE_ECO8A]] Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol (By similarity).
| + | [https://www.uniprot.org/uniprot/ISPE_ECOLI ISPE_ECOLI] Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol (PubMed:10570138, PubMed:10655484, Ref.6). Phosphorylates isopentenyl phosphate at low rates. Also acts on isopentenol, and, much less efficiently, dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a substrate (PubMed:10570138).<ref>PMID:10570138</ref> <ref>PMID:10655484</ref> [REFERENCE:6] |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gabrielsen, M]] | + | [[Category: Gabrielsen M]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Hunter WN]] |
| - | [[Category: Kalinowska-Tluscik, J]] | + | [[Category: Kalinowska-Tluscik J]] |
| - | [[Category: Leonard, G A]] | + | [[Category: Leonard GA]] |
| - | [[Category: McSweeney, S M]] | + | [[Category: McSweeney SM]] |
| - | [[Category: Miallau, L]] | + | [[Category: Miallau L]] |
| - | [[Category: Isoprenoid biosynthesis]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Non-mevalonate pathway]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ISPE_ECOLI Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol (PubMed:10570138, PubMed:10655484, Ref.6). Phosphorylates isopentenyl phosphate at low rates. Also acts on isopentenol, and, much less efficiently, dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a substrate (PubMed:10570138).[1] [2] [REFERENCE:6]
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
4-Diphosphocytidyl-2C-methyl-D-erythritol kinase (IspE; EC 2.7.1.148) contributes to the 1-deoxy-D-xylulose 5-phosphate or mevalonate-independent biosynthetic pathway that produces the isomers isopentenyl diphosphate and dimethylallyl diphosphate. These five-carbon compounds are the fundamental building blocks for the biosynthesis of isoprenoids. The mevalonate-independent pathway does not occur in humans, but is present and has been shown to be essential in many dangerous pathogens, i.e. Plasmodium species, which cause malaria, and gram-negative bacteria. Thus, the enzymes involved in this pathway have attracted attention as potential drug targets. IspE produces 4-diphosphosphocytidyl-2C-methyl-D-erythritol 2-phosphate by ATP-dependent phosphorylation of 4-diphosphocytidyl-2C-methyl-D-erythritol. A triclinic crystal structure of the Escherichia coli IspE-ADP complex with two molecules in the asymmetric unit was determined at 2 A resolution and compared with a monoclinic crystal form of a ternary complex of E. coli IspE also with two molecules in the asymmetric unit. The molecular packing is different in the two forms. In the asymmetric unit of the triclinic crystal form the substrate-binding sites of IspE are occluded by structural elements of the partner, suggesting that the ;triclinic dimer' is an artefact of the crystal lattice. The surface area of interaction in the triclinic form is almost double that observed in the monoclinic form, implying that the dimeric assembly in the monoclinic form may also be an artifact of crystallization.
A triclinic crystal form of Escherichia coli 4-diphosphocytidyl-2C-methyl-D-erythritol kinase and reassessment of the quaternary structure.,Kalinowska-Tluscik J, Miallau L, Gabrielsen M, Leonard GA, McSweeney SM, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt, 3):237-41. Epub 2010 Feb 23. PMID:20208151[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lange BM, Croteau R. Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13714-9. PMID:10570138 doi:10.1073/pnas.96.24.13714
- ↑ Lüttgen H, Rohdich F, Herz S, Wungsintaweekul J, Hecht S, Schuhr CA, Fellermeier M, Sagner S, Zenk MH, Bacher A, Eisenreich W. Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1062-7. PMID:10655484 doi:10.1073/pnas.97.3.1062
- ↑ Kalinowska-Tluscik J, Miallau L, Gabrielsen M, Leonard GA, McSweeney SM, Hunter WN. A triclinic crystal form of Escherichia coli 4-diphosphocytidyl-2C-methyl-D-erythritol kinase and reassessment of the quaternary structure. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt, 3):237-41. Epub 2010 Feb 23. PMID:20208151 doi:10.1107/S1744309109054591
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