1FPS

CRYSTAL STRUCTURE OF RECOMBINANT FARNESYL DIPHOSPHATE SYNTHASE AT 2.6 ANGSTROMS RESOLUTION

1FPS の概要

• エントリーDOI: 10.2210/pdb1fps/pdb
• 分子名称: FARNESYL DIPHOSPHATE SYNTHASE (2 entities in total)
• 機能のキーワード: prenyltransferase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cytoplasm: P08836
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40020.73

構造登録者

Tarshis, L.C.,Yan, M.,Poulter, C.D.,Sacchettini, J.C. (登録日: 1994-06-30, 公開日: 1995-07-10, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)