9PZK
Crystal structure of Petunia x hybrida benzaldehyde synthase in complex with NADP
Summary for 9PZK
| Entry DOI | 10.2210/pdb9pzk/pdb |
| Descriptor | Benzaldehyde synthase, alpha subunit, Benzaldehyde synthase, beta subunit, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | nadp+ bound, heterotetrameric, plant protein |
| Biological source | Petunia x hybrida More |
| Total number of polymer chains | 8 |
| Total formula weight | 245596.05 |
| Authors | Matos, J.O.,Prem Kumar, R.,Weng, J.K. (deposition date: 2025-08-11, release date: 2026-07-01, Last modification date: 2026-08-12) |
| Primary citation | Matos, J.O.,Lee, J.,Kumar, R.P.,Huang, X.Q.,Bergman, M.E.,Sherk, J.,Keswani, V.,Dudareva, N.,Weng, J.K. Structural and mechanistic basis for the heterotetrameric benzaldehyde synthase from petunia. Sci Adv, 12:eaec7733-eaec7733, 2026 Cited by PubMed Abstract: Benzaldehyde is a widespread volatile compound produced by plants. Its final biosynthetic step is catalyzed by benzaldehyde synthase (BS), a peroxisomal enzyme composed of α and β subunits, both belonging to the short-chain dehydrogenase/reductase (SDR) family. Here, we report the crystal structure of BS, which reveals an αβ heterotetrameric arrangement. Structural and biochemical analyses show that the α subunits contain the canonical catalytic site, whereas the β subunits have lost catalytic activity but are essential for heterotetramer assembly. Notably, the C terminus of the β subunit extends into the diagonally positioned α subunit, contributing to the formation of the composite benzoyl-CoA substrate-binding pocket. Site-directed mutagenesis and subunit-mixing experiments support noncooperative, additive contributions of protomers within the heterotetramer. This work establishes BS as a rare heterotetrameric plant SDR and demonstrates how subunit specialization and intersubunit arrangement enable function, providing principles for understanding and engineering multimeric enzyme complexes. PubMed: 42525737DOI: 10.1126/sciadv.aec7733 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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