7YGK

Crystal structure of a secretory phospholipase A2 from Sciscionella marina

Summary for 7YGK

• Entry DOI: 10.2210/pdb7ygk/pdb
• Descriptor: phospholipase A2 (2 entities in total)
• Functional Keywords: phospholipase a2, sciscionella marina, thermostability, loop anchoring, hydrolase
• Biological source: Sciscionella marina
• Total number of polymer chains: 1
• Total formula weight: 13124.31

Authors

Kang, B.G.,Cha, S.S. (deposition date: 2022-07-11, release date: 2023-02-22, Last modification date: 2024-10-16)

Primary citation

Kang, B.G.,Kwon, S.Y.,Lee, H.R.,Hwang, Y.,Youn, S.Y.,Oh, C.,Park, J.B.,Cha, S.S.
Structural and functional characterization of a thermostable secretory phospholipase A 2 from Sciscionella marina and its application in liposome biotransformation.
Acta Crystallogr D Struct Biol, 79:188-197, 2023

PubMed Abstract: Secretory phospholipase A (sPLA), which hydrolyzes the sn-2 acyl bond of lecithin in a Ca-dependent manner, is an important enzyme in the oil and oleochemical industries. However, most sPLAs are not stable under process conditions. Therefore, a thermostable sPLA was investigated in this study. A marine bacterial sPLA isolated from Sciscionella marina (Sm-sPLA) was catalytically active even after 5 h of incubation at high temperatures of up to 50°C, which is outstanding compared with a representative bacterial sPLA (i.e. sPLA from Streptomyces violaceoruber; Sv-sPLA). Consistent with this, the melting temperature of Sm-sPLA was measured to be 7.7°C higher than that of Sv-sPLA. Furthermore, Sm-sPLA exhibited an improved biotransformation performance compared with Sv-sPLA in the hydrolysis of soy lecithin to lysolecithin and free fatty acids at 50°C. Structural and mutagenesis studies revealed that the Trp41-mediated anchoring of a Ca-binding loop into the rest of the protein body is directly linked to the thermal stability of Sm-sPLA. This finding provides a novel structural insight into the thermostability of sPLA and could be applied to create mutant proteins with enhanced industrial potential.

PubMed: 36762864
DOI: 10.1107/S2059798323000384

Experimental method

X-RAY DIFFRACTION (1.24 Å)