Hou_2016_Insect.Biochem.Mol.Biol_68_79

Reference

Title : Crystal structure of vespid phospholipase A1 reveals insights into the mechanism for cause of membrane dysfunction - Hou_2016_Insect.Biochem.Mol.Biol_68_79
Author(s) : Hou MH , Chuang CY , Ko TP , Hu NJ , Chou CC , Shih YP , Ho CL , Wang AH
Ref : Insect Biochemistry & Molecular Biology , 68 :79 , 2016
Abstract :

Vespid phospholipase A1 (vPLA1) from the black-bellied hornet (Vespa basalis) catalyzes the hydrolysis of emulsified phospholipids and shows potent hemolytic activity that is responsible for its lethal effect. To investigate the mechanism of vPLA1 towards its function such as hemolysis and emulsification, we isolated vPLA1 from V. basalis venom and determined its crystal structure at 2.5 A resolution. vPLA1 belongs to the alpha/beta hydrolase fold family. It contains a tightly packed beta-sheet surrounded by ten alpha-helices and a Gly-X-Ser-X-Gly motif, characteristic of a serine hydrolyase active site. A bound phospholipid was modeled into the active site adjacent to the catalytic Ser-His-Asp triad indicating that Gln95 is located at hydrogen-bonding distance from the substrate's phosphate group. Moreover, a hydrophobic surface comprised by the side chains of Phe53, Phe62, Met91, Tyr99, Leu197, Ala167 and Pro169 may serve as the acyl chain-binding site. vPLA1 shows global similarity to the N-terminal domain of human pancreatic lipase (HPL), but with some local differences. The lid domain and the beta9 loop responsible for substrate selectivity in vPLA1 are shorter than in HPL. Thus, solvent-exposed hydrophilic residues can easily accommodate the polar head groups of phospholipids, thereby accounting for the high activity level of vPLA1. Our result provides a potential explanation for the ability of vPLA1 to hydrolyze phospholipids of cell membrane.

PubMedSearch : Hou_2016_Insect.Biochem.Mol.Biol_68_79
PubMedID: 26603193
Gene_locus related to this paper: vesba-pa1

Related information

Gene_locus vesba-pa1
Family vesba-pa1    Insect_Phospholipase
Structure vesba-pa1    Insect_Phospholipase    4QNN

Citations formats

Hou MH, Chuang CY, Ko TP, Hu NJ, Chou CC, Shih YP, Ho CL, Wang AH (2016)
Crystal structure of vespid phospholipase A1 reveals insights into the mechanism for cause of membrane dysfunction
Insect Biochemistry & Molecular Biology 68 :79

Hou MH, Chuang CY, Ko TP, Hu NJ, Chou CC, Shih YP, Ho CL, Wang AH (2016)
Insect Biochemistry & Molecular Biology 68 :79