7WMD

PQQ-dependent alcohol dehydrogenase detoxifying DON

Summary for 7WMD

• Entry DOI: 10.2210/pdb7wmd/pdb
• Descriptor: PQQ-dependent alcohol dehydrogenase, CALCIUM ION (3 entities in total)
• Functional Keywords: dehydrogenase, pqq, toxin
• Biological source: Devosia albogilva
• Total number of polymer chains: 1
• Total formula weight: 62028.64

Authors

Chen, M.,Yang, H.,Lv, F. (deposition date: 2022-01-14, release date: 2022-09-07, Last modification date: 2024-10-09)

Primary citation

Yang, H.,Yan, R.,Li, Y.,Lu, Z.,Bie, X.,Zhao, H.,Lu, F.,Chen, M.
Structure-Function Analysis of a Quinone-Dependent Dehydrogenase Capable of Deoxynivalenol Detoxification.
J.Agric.Food Chem., 70:6764-6774, 2022

PubMed Abstract: The pyrroloquinoline quinone (PQQ)-dependent dehydrogenase DepA detoxifies deoxynivalenol (DON) by converting the C3-OH into a keto group. Herein, two crystal structures of DepA and its complex with PQQ were determined, together with biochemical evidence confirming the interactions of DepA with PQQ and DON and revealing a unique tyrosine residue important for substrate selection. Furthermore, four loops over the active site essential for DepA activity were identified, of which three loops were stabilized by PQQ, and the fourth loop invisible in both structures was considered important for binding DON, together constituting a lid for the active site. Preliminary engineering of the loop showed its potential for enzyme improvement. This study provides structural insights into how a PQQ-dependent dehydrogenase is equipped with the function of DON conversion and for the first time shows the necessity of a lid structure for PQQ-dependent dehydrogenase activity, laying foundation for structure-based design to enhance catalysis efficiency.

PubMed: 35613468
DOI: 10.1021/acs.jafc.2c01083

Experimental method

X-RAY DIFFRACTION (2 Å)