8WD5

Crystal structure of farnesyl diphosphate synthase FPPS1 from silkworm, Bombyx mori

Summary for 8WD5

• Entry DOI: 10.2210/pdb8wd5/pdb
• Descriptor: Farnesyl pyrophosphate synthase, GLYCEROL (3 entities in total)
• Functional Keywords: mevalonate pathway; jh biosynthesis; terpenoids production; lepidopteran fpps, biosynthetic protein
• Biological source: Bombyx mori (domestic silkworm)
• Total number of polymer chains: 2
• Total formula weight: 85231.84

Authors

Guo, P.C.,Fang, H. (deposition date: 2023-09-14, release date: 2024-05-22)

Primary citation

Fang, H.,Zheng, H.,Yang, Y.,Hu, Y.,Wang, Z.,Xia, Q.,Guo, P.
Structural Insights into the Substrate Binding of Farnesyl Diphosphate Synthase FPPS1 from Silkworm, Bombyx mori.
J.Agric.Food Chem., 72:1787-1796, 2024

PubMed Abstract: Farnesyl diphosphate synthase (FPPS) is an important enzyme involved in the juvenile hormone (JH) biosynthesis pathway. Herein, we report the crystal structure of a type-I Lepidopteran FPPS from (FPPS1) at 2.80 Å resolution. FPPS1 adopts an α-helix structure with a deep cavity at the center of the overall structure. Computational simulations combined with biochemical analysis allowed us to define the binding mode of FPPS1 to its substrates. Structural comparison revealed that FPPS1 adopts a structural pattern similar to that of type-II FPPS but exhibits a distinct substrate-binding site. These findings provide a structural basis for understanding substrate preferences and designing FPPS inhibitors. Furthermore, the expression profiles and RNA interference of FPPSs indicated that they play critical roles in the JH biosynthesis and larval-pupal metamorphosis. These findings enhance our understanding of the structural features of type-I Lepidopteran FPPS while providing direct evidence for the physiological role of FPPSs in silkworm development.

PubMed: 38214248
DOI: 10.1021/acs.jafc.3c06741

Experimental method

X-RAY DIFFRACTION (2.8 Å)