9X0R

Cryo-EM Structure of Alcohol Dehydrogenase Variant from Gluconobacter oxydans Truncating Membrane-Binding Regions (Form 2)

Summary for 9X0R

Entry DOI	10.2210/pdb9x0r/pdb
Related	9X0Q
EMDB information	66440
Descriptor	Alcohol dehydrogenase (quinone), dehydrogenase subunit, Alcohol dehydrogenase (quinone), cytochrome c subunit, Small subunit of alcohol dehydrogenase, ... (6 entities in total)
Functional Keywords	comples, oxidoreductase, membrane-bound protein
Biological source	Gluconobacter oxydans More
Total number of polymer chains	3
Total formula weight	149012.97
Authors	Ichikawa, K.,Adachi, T.,Miyata, T.,Makino, F.,Namba, K.,Kitazumi, Y.,Shirai, O.,Sowa, K. (deposition date: 2025-09-30, release date: 2026-08-26)
Primary citation	Ichikawa, K.,Adachi, T.,Miyata, T.,Makino, F.,Namba, K.,Kitazumi, Y.,Shirai, O.,Sowa, K. Structure-guided engineering of membrane-binding regions for surfactant-free solubilization of direct electron transfer-type alcohol dehydrogenase. Chem.Commun.(Camb.), 62:7948-7952, 2026 Cited by PubMed Abstract: Membrane-bound alcohol dehydrogenase (ADH) from is a direct electron transfer-type biocatalyst for ethanol oxidation. To improve its bioelectrocatalysis, membrane-binding regions of ADH were predicted, resulting in the construction of a soluble ADH variant by enzyme engineering. The variant was purified and characterized using structural and bioelectrochemical approaches. PubMed: 41853871 DOI: 10.1039/d6cc00143b PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (2.69 Å)

Structure validation