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| [[Image:1fps.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1fps.png|left|200px]] |
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| {{STRUCTURE_1fps| PDB=1fps | SCENE= }} | | {{STRUCTURE_1fps| PDB=1fps | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF RECOMBINANT FARNESYL DIPHOSPHATE SYNTHASE AT 2.6 ANGSTROMS RESOLUTION'''
| | ===CRYSTAL STRUCTURE OF RECOMBINANT FARNESYL DIPHOSPHATE SYNTHASE AT 2.6 ANGSTROMS RESOLUTION=== |
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| ==Overview==
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| The synthesis of farnesyl diphosphate (FPP), a key intermediate in the isoprenoid biosynthetic pathway required for the synthesis of cholesterol and in the formation of prenylated proteins, is catalyzed by the enzyme farnesyl diphosphate synthase (FPS). The crystal structure of avian recombinant FPS, the first three-dimensional structure for any prenyltransferase, was determined to 2.6-A resolution. The enzyme exhibits a novel fold composed entirely of alpha-helices joined by connecting loops. The enzyme's most prominent structural feature is the arrangement of 10 core helices around a large central cavity. Two aspartate-rich sequences that are highly conserved among the isoprenyl diphosphate synthase family of prenyltransferases, and are essential for enzymatic activity, were found on opposite walls of this cavity, with the aspartate side chains approximately 12 A apart and facing each other. The location and metal ion binding properties of these sequences suggest that the conserved aspartate residues participate in substrate binding of catalysis. | | The line below this paragraph, {{ABSTRACT_PUBMED_8086404}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8086404 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8086404}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Yan, M.]] | | [[Category: Yan, M.]] |
| [[Category: Prenyltransferase]] | | [[Category: Prenyltransferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:37:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:45:14 2008'' |
