6AL3

Lys49 PLA2 BPII derived from the venom of Protobothrops flavoviridis.

Summary for 6AL3

• Entry DOI: 10.2210/pdb6al3/pdb
• Descriptor: Basic phospholipase A2 BP-II, SULFATE ION (2 entities in total)
• Functional Keywords: phospholipase a2, toxic components, nake venom, toxin
• Biological source: Protobothrops flavoviridis (Habu)
• Total number of polymer chains: 4
• Total formula weight: 55445.01

Authors

Matsui, T.,Kamata, S.,Suzuki, A.,Oda-Ueda, N.,Ogawa, T.,Tanaka, Y. (deposition date: 2018-09-05, release date: 2019-01-16, Last modification date: 2024-10-09)

Primary citation

Matsui, T.,Kamata, S.,Ishii, K.,Maruno, T.,Ghanem, N.,Uchiyama, S.,Kato, K.,Suzuki, A.,Oda-Ueda, N.,Ogawa, T.,Tanaka, Y.
SDS-induced oligomerization of Lys49-phospholipase A2from snake venom.
Sci Rep, 9:2330-2330, 2019

PubMed Abstract: Phospholipase A (PLA) is one of the representative toxic components of snake venom. PLAs are categorized into several subgroups according to the amino acid at position 49, which comprises either Asp49, Lys49, Arg49 or Ser49. Previous studies suggested that the Lys49-PLA assembles into an extremely stable dimer. Although the behavior on Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing or non-reducing conditions suggested the presence of intermolecular disulfide bonds, these bonds were not observed in the crystal structure of Lys49-PLA. The reason for this discrepancy between the crystal structure and SDS-PAGE of Lys49-PLA remains unknown. In this study, we analyzed a Lys49-PLA homologue from Protobothrops flavoviridis (PflLys49-PLA BPII), by biophysical analyses including X-ray crystallography, SDS-PAGE, native-mass spectrometry, and analytical ultracentrifugation. The results demonstrated that PflLys49-PLA BPII spontaneously oligomerized in the presence of SDS, which is one of the strongest protein denaturants.

PubMed: 30787342
DOI: 10.1038/s41598-019-38861-8

Experimental method

X-RAY DIFFRACTION (2.57 Å)