8C54
Cryo-EM structure of NADH bound SLA dehydrogenase RlGabD from Rhizobium leguminosarum bv. trifolii SRD1565
Summary for 8C54
| Entry DOI | 10.2210/pdb8c54/pdb |
| EMDB information | 16433 |
| Descriptor | Succinate semialdehyde dehydrogenase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | sulfolactaldehyde dehydrogenase nadh gabd, oxidoreductase |
| Biological source | Rhizobium leguminosarum bv. trifolii SRDI565 |
| Total number of polymer chains | 4 |
| Total formula weight | 213451.18 |
| Authors | Sharma, M.,Meek, R.W.,Armstrong, Z.,Blaza, J.N.,Alhifthi, A.,Li, J.,Goddard-Borger, E.D.,Williams, S.J.,Davies, G.J. (deposition date: 2023-01-06, release date: 2023-09-20, Last modification date: 2024-04-10) |
| Primary citation | Li, J.,Sharma, M.,Meek, R.,Alhifthi, A.,Armstrong, Z.,Soler, N.M.,Lee, M.,Goddard-Borger, E.D.,Blaza, J.N.,Davies, G.J.,Williams, S.J. Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum. Chem Sci, 14:11429-11440, 2023 Cited by PubMed Abstract: Sulfolactate (SL) is a short-chain organosulfonate that is an important reservoir of sulfur in the biosphere. SL is produced by oxidation of sulfolactaldehyde (SLA), which in turn derives from sulfoglycolysis of the sulfosugar sulfoquinovose, or through oxidation of 2,3-dihydroxypropanesulfonate. Oxidation of SLA is catalyzed by SLA dehydrogenases belonging to the aldehyde dehydrogenase superfamily. We report that SLA dehydrogenase GabD from the sulfoglycolytic bacterium SRDI565 can use both NAD and NADP as cofactor to oxidize SLA, and indicatively operates through a rapid equilibrium ordered mechanism. We report the cryo-EM structure of GabD bound to NADH, revealing a tetrameric quaternary structure and supporting proposal of organosulfonate binding residues in the active site, and a catalytic mechanism. Sequence based homology searches identified SLA dehydrogenase homologs in a range of putative sulfoglycolytic gene clusters in bacteria predominantly from the phyla Actinobacteria, Firmicutes, and Proteobacteria. This work provides a structural and biochemical view of SLA dehydrogenases to complement our knowledge of SLA reductases, and provide detailed insights into a critical step in the organosulfur cycle. PubMed: 37886098DOI: 10.1039/d3sc01594g PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.52 Å) |
Structure validation
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