3kra
From Proteopedia
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| - | {{STRUCTURE_3kra| PDB=3kra | SCENE= }} | ||
| - | ===Mint heterotetrameric geranyl pyrophosphate synthase in complex with magnesium=== | ||
| - | {{ABSTRACT_PUBMED_20139160}} | ||
| - | == | + | ==Mint heterotetrameric geranyl pyrophosphate synthase in complex with magnesium== |
| - | [[3kra]] is a 4 chain structure with sequence from [ | + | <StructureSection load='3kra' size='340' side='right'caption='[[3kra]], [[Resolution|resolution]] 1.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3kra]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mentha_x_piperita Mentha x piperita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KRA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3kra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kra OCA], [https://pdbe.org/3kra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kra RCSB], [https://www.ebi.ac.uk/pdbsum/3kra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kra ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9SBR3_MENPI Q9SBR3_MENPI] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kr/3kra_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3kra ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Terpenes (isoprenoids), derived from isoprenyl pyrophosphates, are versatile natural compounds that act as metabolism mediators, plant volatiles, and ecological communicators. Divergent evolution of homomeric prenyltransferases (PTSs) has allowed PTSs to optimize their active-site pockets to achieve catalytic fidelity and diversity. Little is known about heteromeric PTSs, particularly the mechanisms regulating formation of specific products. Here, we report the crystal structure of the (LSU . SSU)(2)-type (LSU/SSU = large/small subunit) heterotetrameric geranyl pyrophosphate synthase (GPPS) from mint (Mentha piperita). The LSU and SSU of mint GPPS are responsible for catalysis and regulation, respectively, and this SSU lacks the essential catalytic amino acid residues found in LSU and other PTSs. Whereas no activity was detected for individually expressed LSU or SSU, the intact (LSU . SSU)(2) tetramer produced not only C(10)-GPP at the beginning of the reaction but also C(20)-GGPP (geranylgeranyl pyrophosphate) at longer reaction times. The activity for synthesizing C(10)-GPP and C(20)-GGPP, but not C(15)-farnesyl pyrophosphate, reflects a conserved active-site structure of the LSU and the closely related mustard (Sinapis alba) homodimeric GGPPS. Furthermore, using a genetic complementation system, we showed that no C(20)-GGPP is produced by the mint GPPS in vivo. Presumably through protein-protein interactions, the SSU remodels the active-site cavity of LSU for synthesizing C(10)-GPP, the precursor of volatile C(10)-monoterpenes. | ||
| - | + | Structure of a heterotetrameric geranyl pyrophosphate synthase from mint (Mentha piperita) reveals intersubunit regulation.,Chang TH, Hsieh FL, Ko TP, Teng KH, Liang PH, Wang AH Plant Cell. 2010 Feb;22(2):454-67. Epub 2010 Feb 5. PMID:20139160<ref>PMID:20139160</ref> | |
| - | <ref | + | |
| - | [[Category: | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: | + | </div> |
| - | [[Category: Chang | + | <div class="pdbe-citations 3kra" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hsieh | + | == References == |
| - | [[Category: Ko | + | <references/> |
| - | [[Category: Wang | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Mentha x piperita]] | |
| - | + | [[Category: Chang T-H]] | |
| + | [[Category: Hsieh F-L]] | ||
| + | [[Category: Ko T-P]] | ||
| + | [[Category: Wang AH-J]] | ||
Current revision
Mint heterotetrameric geranyl pyrophosphate synthase in complex with magnesium
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