1FPS

CRYSTAL STRUCTURE OF RECOMBINANT FARNESYL DIPHOSPHATE SYNTHASE AT 2.6 ANGSTROMS RESOLUTION

Summary for 1FPS

• Entry DOI: 10.2210/pdb1fps/pdb
• Descriptor: FARNESYL DIPHOSPHATE SYNTHASE (2 entities in total)
• Functional Keywords: prenyltransferase
• Biological source: Gallus gallus (chicken)
• Cellular location: Cytoplasm: P08836
• Total number of polymer chains: 1
• Total formula weight: 40020.73

Authors

Tarshis, L.C.,Yan, M.,Poulter, C.D.,Sacchettini, J.C. (deposition date: 1994-06-30, release date: 1995-07-10, Last modification date: 2024-02-07)

Primary citation

Tarshis, L.C.,Yan, M.,Poulter, C.D.,Sacchettini, J.C.
Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution.
Biochemistry, 33:10871-10877, 1994

PubMed Abstract: 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.

PubMed: 8086404
DOI: 10.1021/bi00202a004

Experimental method

X-RAY DIFFRACTION (2.6 Å)