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| <StructureSection load='3noy' size='340' side='right'caption='[[3noy]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3noy' size='340' side='right'caption='[[3noy]], [[Resolution|resolution]] 2.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3noy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NOY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3noy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NOY FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.7Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ke8|3ke8]], [[3dnf|3dnf]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aq_1540, gcpE, ispG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr> | + | |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate_synthase (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.7.1 1.17.7.1] </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=3noy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3noy OCA], [https://pdbe.org/3noy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3noy RCSB], [https://www.ebi.ac.uk/pdbsum/3noy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3noy 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=3noy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3noy OCA], [https://pdbe.org/3noy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3noy RCSB], [https://www.ebi.ac.uk/pdbsum/3noy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3noy ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/ISPG_AQUAE ISPG_AQUAE]] Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.<ref>PMID:20932974</ref>
| + | [https://www.uniprot.org/uniprot/ISPG_AQUAE ISPG_AQUAE] Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.<ref>PMID:20932974</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Bacher, A]] | + | [[Category: Bacher A]] |
- | [[Category: Graewert, T]] | + | [[Category: Graewert T]] |
- | [[Category: Groll, M]] | + | [[Category: Groll M]] |
- | [[Category: Converts 2c-methyl-d-erythritol 2]]
| + | |
- | [[Category: Cytosol]]
| + | |
- | [[Category: Ferredoxin c-domain]]
| + | |
- | [[Category: Iron-sulfur protein]]
| + | |
- | [[Category: Isoprenoid biosynthesis]]
| + | |
- | [[Category: Non-mevalonate pathway]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Terpene biosynthesis]]
| + | |
- | [[Category: Tim-barrel n-domain]]
| + | |
| Structural highlights
Function
ISPG_AQUAE Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.[1]
Publication Abstract from PubMed
IspG protein serves as the penultimate enzyme of the recently discovered non-mevalonate pathway for the biosynthesis of the universal isoprenoid precursors, isopentenyl diphosphate and dimethylallyl diphosphate. The enzyme catalyzes the reductive ring opening of 2C-methyl-d-erythritol 2,4-cyclodiphosphate, which affords 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. The protein was crystallized under anaerobic conditions, and its three-dimensional structure was determined to a resolution of 2.7 A. Each subunit of the c(2) symmetric homodimer folds into two domains connected by a short linker sequence. The N-terminal domain (N domain) is an eight-stranded beta barrel that belongs to the large TIM-barrel superfamily. The C-terminal domain (C domain) consists of a beta sheet that is flanked on both sides by helices. One glutamate and three cysteine residues of the C domain coordinate a [4Fe-4S] cluster. Homodimer formation involves an extended contact area (about 1100 A(2)) between helices 8 and 9 of each respective beta barrel. Moreover, each C domain contacts the N domain of the partner subunit, but the interface regions are small (about 430 A(2)). We propose that the enzyme substrate binds to the positively charged surface area at the C-terminal pole of the beta barrel. The C domain carrying the iron-sulfur cluster could then move over to form a closed conformation where the substrate is sandwiched between the N domain and the C domain. This article completes the set of three-dimensional structures of the non-mevalonate pathway enzymes, which are of specific interest as potential targets for tuberculostatic and antimalarial drugs.
Biosynthesis of Isoprenoids: Crystal Structure of the [4Fe-4S] Cluster Protein IspG.,Lee M, Grawert T, Quitterer F, Rohdich F, Eppinger J, Eisenreich W, Bacher A, Groll M J Mol Biol. 2010 Oct 7. PMID:20932974[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee M, Grawert T, Quitterer F, Rohdich F, Eppinger J, Eisenreich W, Bacher A, Groll M. Biosynthesis of Isoprenoids: Crystal Structure of the [4Fe-4S] Cluster Protein IspG. J Mol Biol. 2010 Oct 7. PMID:20932974 doi:10.1016/j.jmb.2010.09.050
- ↑ Lee M, Grawert T, Quitterer F, Rohdich F, Eppinger J, Eisenreich W, Bacher A, Groll M. Biosynthesis of Isoprenoids: Crystal Structure of the [4Fe-4S] Cluster Protein IspG. J Mol Biol. 2010 Oct 7. PMID:20932974 doi:10.1016/j.jmb.2010.09.050
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