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5mrp
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Arabidopsis thaliana IspD Glu258Ala mutant in complex with Azolopyrimidine (2)== | |
| + | <StructureSection load='5mrp' size='340' side='right' caption='[[5mrp]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mrp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MRP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6BC:5-CHLORO-7-HYDROXY-6-(PHENYLMETHYL)PYRAZOLO[1,5-A]PYRIMIDINE-3-CARBONITRILE'>6BC</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w77|1w77]], [[2yc5|2yc5]], [[4nak|4nak]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-C-methyl-D-erythritol_4-phosphate_cytidylyltransferase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.60 2.7.7.60] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mrp OCA], [http://pdbe.org/5mrp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mrp RCSB], [http://www.ebi.ac.uk/pdbsum/5mrp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mrp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ISPD_ARATH ISPD_ARATH]] Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). Is essential for chloroplast development and required for pigments and gibberellins biosynthesis.<ref>PMID:10841550</ref> <ref>PMID:12029484</ref> <ref>PMID:18236010</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzymes of the nonmevalonate pathway of isoprenoid biosynthesis are attractive targets for the development of herbicides and drugs against infectious diseases. While this pathway is essential for many pathogens and plants, mammals do not depend on it for the synthesis of isoprenoids. IspD, the third enzyme of the nonmevalonate pathway, is unique in that it has an allosteric regulatory site. We elucidated the binding mode of phenylisoxazoles, a new class of allosteric inhibitors. Allosteric inhibition is effected by large conformational changes of a loop region proximal to the active site. We investigated the different roles of residues in this loop by mutation studies and identified repulsive interactions with Asp291 and Asp292 to be responsible for inhibition. Crystallographic data and the response of mutant enzymes to three different classes of allosteric inhibitors provide an in-depth understanding of the allosteric mechanism. The obtained mutant enzymes show selective resistance to allosteric inhibitors and provide conceptually valuable information for future engineering of herbicide-resistant crops. We found that the isoprenoid precursors IPP and DMAPP are natural inhibitors of Arabidopsis thaliana IspD; however, they do not seem to bind to the allosteric site. | ||
| - | + | Mechanism of Allosteric Inhibition of the Enzyme IspD by Three Different Classes of Ligands.,Schwab A, Illarionov B, Frank A, Kunfermann A, Seet M, Bacher A, Witschel MC, Fischer M, Groll M, Diederich F ACS Chem Biol. 2017 Aug 18;12(8):2132-2138. doi: 10.1021/acschembio.7b00004. Epub, 2017 Jul 7. PMID:28686408<ref>PMID:28686408</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5mrp" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | [[ | + | ==See Also== |
| - | [[Category: | + | *[[MEP cytidylyltransferase|MEP cytidylyltransferase]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase]] | ||
[[Category: Bacher, A]] | [[Category: Bacher, A]] | ||
| - | [[Category: Seet, M]] | ||
[[Category: Diederich, F]] | [[Category: Diederich, F]] | ||
| + | [[Category: Fischer, M]] | ||
| + | [[Category: Frank, A]] | ||
[[Category: Groll, M]] | [[Category: Groll, M]] | ||
[[Category: Illarionov, B]] | [[Category: Illarionov, B]] | ||
| + | [[Category: Kunfermann, A]] | ||
| + | [[Category: Schwab, A]] | ||
| + | [[Category: Seet, M]] | ||
[[Category: Witschel, M]] | [[Category: Witschel, M]] | ||
| + | [[Category: Allosteric inhibition]] | ||
| + | [[Category: Anti-infective]] | ||
| + | [[Category: Drug discovery]] | ||
| + | [[Category: Herbicide]] | ||
| + | [[Category: Mutant]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 04:11, 30 August 2017
Arabidopsis thaliana IspD Glu258Ala mutant in complex with Azolopyrimidine (2)
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