2e94: Difference between revisions

Revision as of 15:36, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2e94.png

Template:STRUCTURE 2e94

S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and BPH-364S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and BPH-364

Template:ABSTRACT PUBMED 17535895

About this StructureAbout this Structure

2E94 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and BPH-364'''
+===S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and BPH-364===
-==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.
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 ==About this Structure==
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 [[Category: Farnesyl pyrophosphate]]
 [[Category: Prenyltransferase]]
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