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| [[Image:2e90.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2e90| PDB=2e90 | SCENE= }} | | {{STRUCTURE_2e90| PDB=2e90 | SCENE= }} |
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| '''S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium, pyrophosphate and FPP'''
| | ===S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium, pyrophosphate and FPP=== |
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| ==Overview==
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| Bisphosphonate 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17535895}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17535895 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17535895}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Farnesyl pyrophosphate]] | | [[Category: Farnesyl pyrophosphate]] |
| [[Category: Prenyltransferase]] | | [[Category: Prenyltransferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:09:51 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:58:59 2008'' |