2e90: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2e90]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E90 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2e90]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E90 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dh4|2dh4]], [[2e8t|2e8t]], [[2e8u|2e8u]], [[2e8v|2e8v]], [[2e8w|2e8w]], [[2e8x|2e8x]], [[2e91|2e91]], [[2e92|2e92]], [[2e93|2e93]], [[2e94|2e94]], [[2e95|2e95]], [[2e96|2e96]], [[2e97|2e97]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dh4|2dh4]], [[2e8t|2e8t]], [[2e8u|2e8u]], [[2e8v|2e8v]], [[2e8w|2e8w]], [[2e8x|2e8x]], [[2e91|2e91]], [[2e92|2e92]], [[2e93|2e93]], [[2e94|2e94]], [[2e95|2e95]], [[2e96|2e96]], [[2e97|2e97]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-hexaprenyltranstransferase Trans-hexaprenyltranstransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.30 2.5.1.30] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-hexaprenyltranstransferase Trans-hexaprenyltranstransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.30 2.5.1.30] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e90 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e90 RCSB], [http://www.ebi.ac.uk/pdbsum/2e90 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=2e90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e90 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e90 RCSB], [http://www.ebi.ac.uk/pdbsum/2e90 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/GGPPS_YEAST GGPPS_YEAST]] Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of YPT1 and SEC4. May be involved in vesicle trafficking and protein sorting.<ref>PMID:7665600</ref> <ref>PMID:15296494</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Trans-hexaprenyltranstransferase]] | [[Category: Trans-hexaprenyltranstransferase]] | ||
[[Category: Chang, T H | [[Category: Chang, T H]] | ||
[[Category: Chen, C K.M | [[Category: Chen, C K.M]] | ||
[[Category: Guo, R T | [[Category: Guo, R T]] | ||
[[Category: Jeng, W Y | [[Category: Jeng, W Y]] | ||
[[Category: Ko, T P | [[Category: Ko, T P]] | ||
[[Category: Liang, P H | [[Category: Liang, P H]] | ||
[[Category: Oldfield, E | [[Category: Oldfield, E]] | ||
[[Category: Wang, A H.J | [[Category: Wang, A H.J]] | ||
[[Category: Bisphosphonate]] | [[Category: Bisphosphonate]] | ||
[[Category: Farnesyl pyrophosphate]] | [[Category: Farnesyl pyrophosphate]] | ||
[[Category: Prenyltransferase]] | [[Category: Prenyltransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 01:25, 26 December 2014
S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium, pyrophosphate and FPPS. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium, pyrophosphate and FPP
Structural highlights
Function[GGPPS_YEAST] Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of YPT1 and SEC4. May be involved in vesicle trafficking and protein sorting.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBisphosphonate drugs (e.g., Fosamax and Zometa) are thought to act primarily by inhibiting farnesyl diphosphate synthase (FPPS), resulting in decreased prenylation of small GTPases. Here, we show that some bisphosphonates can also inhibit geranylgeranyl diphosphate synthase (GGPPS), as well as undecaprenyl diphosphate synthase (UPPS), a cis-prenyltransferase of interest as a target for antibacterial therapy. Our results on GGPPS (10 structures) show that there are three bisphosphonate-binding sites, consisting of FPP or isopentenyl diphosphate substrate-binding sites together with a GGPP product- or inhibitor-binding site. In UPPS, there are a total of four binding sites (in five structures). These results are of general interest because they provide the first structures of GGPPS- and UPPS-inhibitor complexes, potentially important drug targets, in addition to revealing a remarkably broad spectrum of binding modes not seen in FPPS inhibition. Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases.,Guo RT, Cao R, Liang PH, Ko TP, Chang TH, Hudock MP, Jeng WY, Chen CK, Zhang Y, Song Y, Kuo CJ, Yin F, Oldfield E, Wang AH Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10022-7. Epub 2007 May 29. PMID:17535895[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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