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==Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor== | ==Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor== | ||
<StructureSection load='3cp6' size='340' side='right' caption='[[3cp6]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3cp6' size='340' side='right' caption='[[3cp6]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cp6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3cp6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CP6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RSX:(4AS,7AR)-OCTAHYDRO-1H-CYCLOPENTA[B]PYRIDINE-6,6-DIYLBIS(PHOSPHONIC+ACID)'>RSX</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RSX:(4AS,7AR)-OCTAHYDRO-1H-CYCLOPENTA[B]PYRIDINE-6,6-DIYLBIS(PHOSPHONIC+ACID)'>RSX</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yq7|1yq7]], [[2qis|2qis]], [[1zw5|1zw5]], [[1yv5|1yv5]], [[3b7l|3b7l]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yq7|1yq7]], [[2qis|2qis]], [[1zw5|1zw5]], [[1yv5|1yv5]], [[3b7l|3b7l]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FDPS, FPS, KIAA1293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FDPS, FPS, KIAA1293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cp6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cp6 RCSB], [http://www.ebi.ac.uk/pdbsum/3cp6 PDBsum]</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=3cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cp6 OCA], [http://pdbe.org/3cp6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cp6 RCSB], [http://www.ebi.ac.uk/pdbsum/3cp6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cp6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=3cp6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| Line 25: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Barnett, B L]] | [[Category: Barnett, B L]] | ||
Revision as of 20:16, 5 August 2016
Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitorCrystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor
Structural highlights
Function[FPPS_HUMAN] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Arrowsmith, C H
- Barnett, B L
- Bountra, C
- Delft, F von
- Dunford, J E
- Ebetino, F H
- Edwards, A M
- Guo, K
- Oppermann, U
- Pike, A C.W
- Pilka, E S
- Russell, R G.G
- Structural genomic
- Bisphosphonate
- Cholesterol biosynthesis
- Cholesterol synthesis
- Host-virus interaction isoprene biosynthesis
- Isoprenoid pathway
- Lipid synthesis
- Sgc
- Steroid biosynthesis
- Sterol biosynthesis
- Transferase