Structural highlights
FunctionPublication Abstract from PubMedNonspecific phospholipase C (NPC) plays a pivotal role in hydrolyzing phospholipids, releasing diacylglycerol horizontal line an essential second messenger. Extensive research has elucidated the structure and function of bacterial and plant NPCs, but our understanding of their fungal counterparts remains limited. Here, we present the first crystal structure of a fungal NPC derived from Rasamsonia emersonii (RePLC), unraveling its distinguishable features divergent from other known phospholipase C. Remarkably, the structure of RePLC contains solely the phosphoesterase domain without the crucial C-terminal domain (CTD) found in plant NPCs, although CTD is important for their activity. Through a comparative analysis of structural features among NPCs from diverse species combined with structure-based mutation analyses and bioinformatics methods, we propose a potential molecular mechanism that may universally underlie the catalysis of phospholipid hydrolysis in fungal NPCs. Furthermore, our study sheds light on the captivating evolutionary trajectory of enzymes across diverse species. Crystal Structure of Fungal Nonspecific Phospholipase C Unveils a Distinct Catalytic Mechanism.,Feng C, Fang H, Wang F, Chen W, Xia LC, Lan D, Wang Y J Agric Food Chem. 2023 Nov 1;71(43):16352-16361. doi: 10.1021/acs.jafc.3c05155. , Epub 2023 Oct 6. PMID:37800479[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 08:41, 14 July 2024.