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| | <StructureSection load='4opu' size='340' side='right'caption='[[4opu]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='4opu' size='340' side='right'caption='[[4opu]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4opu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulac Sulac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OPU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OPU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4opu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius_DSM_639 Sulfolobus acidocaldarius DSM 639]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OPU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GRG:GERANYLGERANYL+DIPHOSPHATE'>GRG</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">[[4opc|4opc]], [[4opd|4opd]], [[4opg|4opg]], [[4opi|4opi]], [[4opl|4opl]], [[4opt|4opt]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GRG:GERANYLGERANYL+DIPHOSPHATE'>GRG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Saci_0986 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330779 SULAC])</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=4opu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4opu OCA], [https://pdbe.org/4opu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4opu RCSB], [https://www.ebi.ac.uk/pdbsum/4opu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4opu ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Geranylgeranyl_diphosphate_reductase Geranylgeranyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.83 1.3.1.83] </span></td></tr>
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| - | <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=4opu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4opu OCA], [http://pdbe.org/4opu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4opu RCSB], [http://www.ebi.ac.uk/pdbsum/4opu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4opu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Geranylgeranyl diphosphate reductase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulac]] | + | [[Category: Sulfolobus acidocaldarius DSM 639]] |
| - | [[Category: Adams, P D]] | + | [[Category: Adams PD]] |
| - | [[Category: Keasling, J D]] | + | [[Category: Keasling JD]] |
| - | [[Category: Kung, Y]] | + | [[Category: Kung Y]] |
| - | [[Category: Liu, C]] | + | [[Category: Liu C]] |
| - | [[Category: McAndrew, R P]] | + | [[Category: McAndrew RP]] |
| - | [[Category: Pereira, J H]] | + | [[Category: Pereira JH]] |
| - | [[Category: Xie, X]] | + | [[Category: Xie X]] |
| - | [[Category: Archaeal protein]]
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| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
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| Structural highlights
Publication Abstract from PubMed
The archaeal enzyme geranylgeranyl reductase (GGR) catalyzes hydrogenation of carbon-carbon double bonds to produce the saturated alkyl chains of the organism's unusual isoprenoid-derived cell membrane. Enzymatic reduction of isoprenoid double bonds is of considerable interest both to natural products researchers and to synthetic biologists interested in the microbial production of isoprenoid drug or biofuel molecules. Here we present crystal structures of GGR from Sulfolobus acidocaldarius, including the structure of GGR bound to geranylgeranyl pyrophosphate (GGPP). The structures are presented alongside activity data that depict the sequential reduction of GGPP to H6GGPP via the intermediates H2GGPP and H4GGPP. We then modified the enzyme to generate sequence variants that display increased rates of H6GGPP production or are able to halt the extent of reduction at H2GGPP and H4GGPP. Crystal structures of these variants not only reveal the structural bases for their altered activities; they also shed light onto the catalytic mechanism employed.
Constructing Tailored Isoprenoid Products by Structure-Guided Modification of Geranylgeranyl Reductase.,Kung Y, McAndrew RP, Xie X, Liu CC, Pereira JH, Adams PD, Keasling JD Structure. 2014 Jun 17. pii: S0969-2126(14)00148-8. doi:, 10.1016/j.str.2014.05.007. PMID:24954619[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kung Y, McAndrew RP, Xie X, Liu CC, Pereira JH, Adams PD, Keasling JD. Constructing Tailored Isoprenoid Products by Structure-Guided Modification of Geranylgeranyl Reductase. Structure. 2014 Jun 17. pii: S0969-2126(14)00148-8. doi:, 10.1016/j.str.2014.05.007. PMID:24954619 doi:http://dx.doi.org/10.1016/j.str.2014.05.007
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