6KQU

Crystal structure of phospholipase A2

Summary for 6KQU

• Entry DOI: 10.2210/pdb6kqu/pdb
• Related: 5Y5E
• Descriptor: Group IIE secretory phospholipase A2, GLYCEROL, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: phospholipase a2, mutation, calcium, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 14671.39

Authors

Hou, S.,Xu, T.,Liu, J. (deposition date: 2019-08-18, release date: 2020-08-19, Last modification date: 2024-10-30)

Primary citation

Hou, S.,Zhang, Y.,Xu, J.,Bai, J.,Liu, J.,Xie, J.,Xu, T.
Residue Asn21 acts as a switch for calcium binding to modulate the enzymatic activity of human phospholipase A2 group IIE.
Biochimie, 176:117-121, 2020

PubMed Abstract: Secreted phospholipases A2 (sPLA2) group IIE (GIIE) is involved in several biological events, such as lipid metabolism and possibly inflammation that may mainly depend on its catalytic reaction. We previously showed that Asn21 is a critical residue that contributes to the enzymatic activity of hGIIE, but the underlying mechanism is still not clear. Here, combined with crystal structures and mutagenesis studies of the Asn21Gly mutant, we demonstrate that Asn21 acts as a switch responsible for the calcium binding and the catalytic efficiency. Our results of the atypical feature of calcium binding in hGIIE not only provide clues to understand the molecular basis of its enzymatic activity and physiological function, but also confer improved specificity for potential inhibitor design of sPLA2.

PubMed: 32659444
DOI: 10.1016/j.biochi.2020.07.003

Experimental method

X-RAY DIFFRACTION (2 Å)