(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Holometabola: NE > Hymenoptera: NE > Apocrita: NE > Aculeata: NE > Vespoidea: NE > Vespidae: NE > Vespinae: NE > Vespa: NE > Vespa basalis: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA FNPCPYSDDTVKMIILTRENKKHDFYTLDTIKKHNEFKKSTIKHQVVFIT HGFTSSADTENFLAMAKALSDKGNYLVILIDWRVAACTEEMSGIQLAYYS YAASNTRLVGNYIATVTKMLVQKYNVPMANIRLIGHSLGAHTSGFAGKKV QELGLGKYSEIIGLDPAGPSFKSNDCSERICKTDAHYVQIIHTSNHLGTL VTLGTVDFMNNGYNQPGCGLPLIGETCSHTRAVKYFTECIKHECCLIGVP QSKKPQPVSKCTRNECVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII
References
Title: Crystal structure of vespid phospholipase A1 reveals insights into the mechanism for cause of membrane dysfunction Hou MH, Chuang CY, Ko TP, Hu NJ, Chou CC, Shih YP, Ho CL, Wang AH Ref: Insect Biochemistry & Molecular Biology, 68:79, 2016 : PubMed
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.
Title: Crystallization and preliminary X-ray diffraction analysis of phospholipase A1 isolated from hornet (Vespa basalis) venom Chou CC, Hou MH Ref: Acta Crystallographica Sect F Struct Biol Cryst Commun, 64:1118, 2008 : PubMed
Phospholipase A(1) (PLA(1)) isolated from the black-bellied hornet (Vespa basalis) catalyzes the hydrolysis of emulsified phospholipids in addition to the potent haemolytic activity responsible for its lethal effect. In this study, the crystallization and preliminary crystallographic analysis of PLA(1) from hornet venom with a molecular weight of 32 kDa are reported. PLA(1) was crystallized at 277 K using PEG 4000 as precipitant and a 96.5% complete native data set was collected from a frozen crystal to 2.5 A resolution at 100 K with an overall R(merge) of 6.8%. The crystal belongs to the triclinic space group P1, with unit-cell parameters a = 57.2, b = 70.2, c = 81.6 A, alpha = 107.0, beta = 109.9, gamma = 100.9 degrees . In each asymmetric unit, three or four subunits of PLA(1) are present according to the calculation of the solvent content.
Vespa basalis (hornet) phospholipase A 1 from venom
