8H0C

Structure of the thermolabile hemolysin from Vibrio alginolyticus (in complex with arachidonic acid)

8H0C の概要

• エントリーDOI: 10.2210/pdb8h0c/pdb
• 分子名称: SGNH/GDSL hydrolase family protein, ARACHIDONIC ACID, 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE, ... (5 entities in total)
• 機能のキーワード: vibrio, phospholipase, sgnh hydrolase, gdsl lipase, transferase, thermolabile hemolysin, hydrolase
• 由来する生物種: Vibrio alginolyticus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97513.06

構造登録者

Ma, Q.,Wang, C. (登録日: 2022-09-28, 公開日: 2023-08-16, 最終更新日: 2024-10-30)

主引用文献

Wang, C.,Liu, C.,Zhu, X.,Peng, Q.,Ma, Q.
Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase.
Nat Commun, 14:4795-4795, 2023

PubMed Abstract: Although enzyme catalysis is typified by high specificity, enzymes can catalyze various substrates (substrate promiscuity) and/or different reaction types (catalytic promiscuity) using a single active site. This interesting phenomenon is widely distributed in enzyme catalysis, with both fundamental and applied importance. To date, the mechanistic understanding of enzyme promiscuity is very limited. Herein, we report the structural mechanism underlying the substrate and catalytic promiscuity of Vibrio dual lipase/transferase (VDLT). Crystal structures of the VDLT from Vibrio alginolyticus (ValDLT) and its fatty acid complexes were solved, revealing prominent structural flexibility. In particular, the "Ser-His-Asp" catalytic triad machinery of ValDLT contains an intrinsically flexible oxyanion hole. Analysis of ligand-bound structures and mutagenesis showed that the flexible oxyanion hole and other binding residues can undergo distinct conformational changes to facilitate substrate and catalytic promiscuity. Our study reveals a previously unknown flexible form of the famous catalytic triad machinery and proposes a "catalytic site tuning" mechanism to expand the mechanistic paradigm of enzyme promiscuity.

PubMed: 37558668
DOI: 10.1038/s41467-023-40455-y

実験手法

X-RAY DIFFRACTION (1.98 Å)