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8C54

Cryo-EM structure of NADH bound SLA dehydrogenase RlGabD from Rhizobium leguminosarum bv. trifolii SRD1565

8C54 の概要
エントリーDOI10.2210/pdb8c54/pdb
EMDBエントリー16433
分子名称Succinate semialdehyde dehydrogenase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total)
機能のキーワードsulfolactaldehyde dehydrogenase nadh gabd, oxidoreductase
由来する生物種Rhizobium leguminosarum bv. trifolii SRDI565
タンパク質・核酸の鎖数4
化学式量合計213451.18
構造登録者
Sharma, M.,Meek, R.W.,Armstrong, Z.,Blaza, J.N.,Alhifthi, A.,Li, J.,Goddard-Borger, E.D.,Williams, S.J.,Davies, G.J. (登録日: 2023-01-06, 公開日: 2023-09-20, 最終更新日: 2024-04-10)
主引用文献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: 37886098
DOI: 10.1039/d3sc01594g
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.52 Å)
構造検証レポート
Validation report summary of 8c54
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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