2F6X

Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with sn-G1P and MPD

2F6X の概要

• エントリーDOI: 10.2210/pdb2f6x/pdb
• 関連するPDBエントリー: 1VIZ 2F6U
• 分子名称: (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase, SN-GLYCEROL-1-PHOSPHATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: non-canonical tim-barrel; prenyltransferase; archaeal lipid synthesis; sn-glycerol-1-phosphate; 2-methyl-2, 4-pentanediol; dimer, transferase
• 由来する生物種: Archaeoglobus fulgidus
• 細胞内の位置: Cytoplasm : O29844
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53490.66

構造登録者

Payandeh, J.M. (登録日: 2005-11-29, 公開日: 2006-01-24, 最終更新日: 2024-04-03)

主引用文献

Payandeh, J.,Fujihashi, M.,Gillon, W.,Pai, E.F.
The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme
J.Biol.Chem., 281:6070-6078, 2006

PubMed Abstract: We report crystal structures of the citrate and sn-glycerol-1-phosphate (G1P) complexes of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Archaeoglobus fulgidus (AfGGGPS) at 1.55 and 2.0 A resolution, respectively. AfGGGPS is an enzyme that performs the committed step in archaeal lipid biosynthesis, and it presents the first triose phosphate isomerase (TIM)-barrel structure with a prenyltransferase function. Our studies provide insight into the catalytic mechanism of AfGGGPS and demonstrate how it selects for the sn-G1P isomer. The replacement of "Helix 3" by a "strand" in AfGGGPS, a novel modification to the canonical TIM-barrel fold, suggests a model of enzyme adaptation that involves a "greasy slide" and a "swinging door." We propose functions for the homologous PcrB proteins, which are conserved in a subset of pathogenic bacteria, as either prenyltransferases or being involved in lipoteichoic acid biosynthesis. Sequence and structural comparisons lead us to postulate an early evolutionary history for AfGGGPS, which may highlight its role in the emergence of Archaea.

PubMed: 16377641
DOI: 10.1074/jbc.M509377200

実験手法

X-RAY DIFFRACTION (2 Å)