Protein Family Models

This entry represents a group of bacterial sequences, including the small subunit of the Hexaprenyl diphosphate synthase from Micrococcus luteus (HexPS or HexA), a trans-prenyltransferase that catalyses consecutive head-to-tail condensations of three molecules of isopentenyl diphosphates on a farnesyl diphosphate to form an hexaprenyl diphosphate. HexPS is directly involved in the control of the product chain length. It is composed of mostly antiparallel alpha-helices joined by connecting loops [1]. Paper describing PDB structure 3aqb. [1]. 21068379. Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation. Sasaki D, Fujihashi M, Okuyama N, Kobayashi Y, Noike M, Koyama T, Miki K;. J Biol Chem. 2011;286:3729-3740. Paper describing PDB structure 5h9d. [2]. 27457559. Structure, Function, and Inhibition of Staphylococcus aureus Heptaprenyl Diphosphate Synthase. Desai J, Liu YL, Wei H, Liu W, Ko TP, Guo RT, Oldfield E;. ChemMedChem. 2016;11:1915-1923. (from Pfam)

Date:

2024-10-16

This family contains subunit 1 of heptaprenyl diphosphate synthase (HEPPP synthase) (EC:2.5.1.30) (approximately 230 residues long) from Bacilli. The enzyme consists of two subunits, both of which are required for catalysis of heptaprenyl diphosphate synthesis [1]. This family corresponds to the regulatory subunit [2]. [1]. 9748348. Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex. Zhang YW, Koyama T, Marecak DM, Prestwich GD, Maki Y, Ogura K;. Biochemistry 1998;37:13411-13420. [2]. 27457559. Structure, Function, and Inhibition of Staphylococcus aureus Heptaprenyl Diphosphate Synthase. Desai J, Liu YL, Wei H, Liu W, Ko TP, Guo RT, Oldfield E;. ChemMedChem. 2016;11:1915-1923. (from Pfam)

Date:

2024-10-16