8K3G

Crystal structure of non-specific phospholipase C RePLC (Rasamsonia emersonii)

Summary for 8K3G

• Entry DOI: 10.2210/pdb8k3g/pdb
• Descriptor: Phospholipase C, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: non-specific phospholipase c, hydrolase
• Biological source: Rasamsonia emersonii CBS 393.64
• Total number of polymer chains: 2
• Total formula weight: 103365.59

Authors

Feng, C.H.,Wang, Y.H. (deposition date: 2023-07-15, release date: 2024-07-10)

Primary citation

Feng, C.,Fang, H.,Wang, F.,Chen, W.,Xia, L.C.,Lan, D.,Wang, Y.
Crystal Structure of Fungal Nonspecific Phospholipase C Unveils a Distinct Catalytic Mechanism.
J.Agric.Food Chem., 71:16352-16361, 2023

PubMed Abstract: Nonspecific phospholipase C (NPC) plays a pivotal role in hydrolyzing phospholipids, releasing diacylglycerol─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 (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.

PubMed: 37800479
DOI: 10.1021/acs.jafc.3c05155

Experimental method

X-RAY DIFFRACTION (2.5 Å)