6JKP

Crystal structure of sulfoacetaldehyde reductase from Bifidobacterium kashiwanohense in complex with NAD+

Summary for 6JKP

• Entry DOI: 10.2210/pdb6jkp/pdb
• Descriptor: Methanol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ZINC ION, ... (4 entities in total)
• Functional Keywords: sulfoacetaldehyde reductase nadh, oxidoreductase
• Biological source: Bifidobacterium kashiwanohense PV20-2
• Total number of polymer chains: 4
• Total formula weight: 166268.97

Authors

Zhou, Y.,Xu, T.,Lin, L.,Zhang, Y.,Yuchi, Z. (deposition date: 2019-03-01, release date: 2019-06-12, Last modification date: 2023-11-22)

Primary citation

Zhou, Y.,Wei, Y.,Nanjaraj Urs, A.N.,Lin, L.,Xu, T.,Hu, Y.,Ang, E.L.,Zhao, H.,Yuchi, Z.,Zhang, Y.
Identification and characterization of a new sulfoacetaldehyde reductase from the human gut bacteriumBifidobacterium kashiwanohense.
Biosci.Rep., 39:-, 2019

PubMed Abstract: Hydroxyethylsulfonate (isethionate (Ise)) present in mammalian tissues is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut. In previously studied pathways occurring in environmental bacteria, isethionate is generated by the enzyme sulfoacetaldehyde reductase IsfD, belonging to the short-chain dehydrogenase/reductase (SDR) family. An unrelated sulfoacetaldehyde reductase SarD, belonging to the metal-dependent alcohol dehydrogenase superfamily (M-ADH), was recently discovered in the human gut sulfite-reducing bacterium (SarD). Here we report the structural and biochemical characterization of a sulfoacetaldehyde reductase from the human gut fermenting bacterium (TauF). TauF belongs to the M-ADH family, but is distantly related to SarD (28% sequence identity). The crystal structures of TauF in the apo form and in a binary complex with NAD were determined at 1.9 and 3.0 Å resolution, respectively. Mutagenesis studies were carried out to investigate the involvement of active site residues in binding the sulfonate substrate. Our studies demonstrate the presence of sulfoacetaldehyde reductase in , with a possible role in isethionate production as a byproduct of taurine nitrogen assimilation.

PubMed: 31123167
DOI: 10.1042/BSR20190715

Experimental method

X-RAY DIFFRACTION (3.008 Å)