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''' | ==The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates== | ||
<StructureSection load='4ogu' size='340' side='right' caption='[[4ogu]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ogu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OGU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=210:PAMIDRONATE'>210</scene>, <scene name='pdbligand=IPE:3-METHYLBUT-3-ENYL+TRIHYDROGEN+DIPHOSPHATE'>IPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n9u|4n9u]], [[4ng6|4ng6]], [[1zw5|1zw5]], [[4nua|4nua]]</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=4ogu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ogu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ogu RCSB], [http://www.ebi.ac.uk/pdbsum/4ogu PDBsum]</span></td></tr> | |||
[[Category: | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FPPS_HUMAN 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. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Barnett, B L]] | |||
[[Category: Delft, F Von]] | |||
[[Category: Dunford, J E]] | |||
[[Category: Ebetino, F H]] | |||
[[Category: Muniz, J R.C]] | |||
[[Category: Oppermann, U]] | [[Category: Oppermann, U]] | ||
[[Category: | [[Category: Russell, R G.G]] | ||
[[Category: | [[Category: Tsoumpra, M K]] | ||
[[Category: | [[Category: Walter, R L]] | ||
[[Category: | [[Category: All alpha-helical]] | ||
[[Category: | [[Category: Cholesterol synthesis]] | ||
[[Category: | [[Category: Isoprene biosynthesis]] | ||
[[Category: | [[Category: Isoprenoid pathway]] | ||
[[Category: | [[Category: Lipid biosynthesis]] | ||
[[Category: Prenyltransferase]] | |||
[[Category: Steroid biosynthesis]] | |||
[[Category: Transferase]] | |||
Revision as of 19:57, 21 January 2015
The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonatesThe effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
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. |
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