6ixj

The crystal structure of sulfoacetaldehyde reductase from Klebsiella oxytoca

spinqualitylabelsall models 6ixj, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ixj is a 12 chain structure with sequence from Klebsiella oxytoca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: 8X3, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ISFD_KLEOX Catalyzes the formation of isethionate from 2-sulfoacetaldehyde in the deaminative pathway of taurine. The enzyme is specific for NADPH; NADH is not a substrate. Publication Abstract from PubMed Sulfoacetaldehyde reductase (IsfD) is a member of the short-chain dehydrogenase/reductase (SDR) family, involved in nitrogen assimilation from aminoethylsulfonate (taurine) in certain environmental and human commensal bacteria. IsfD catalyzes the reversible NADPH-dependent reduction of sulfoacetaladehyde, which is generated by transamination of taurine, forming hydroxyethylsulfonate (isethionate) as a waste product. In this study, the crystal structure of Klebsiella oxytoca IsfD in a ternary complex with NADPH and isethionate, was solved at 2.8 A, revealing residues important for substrate binding. IsfD forms a homotetramer in both crystal and solution states, with the C-terminal tail of each subunit interacting with the C-terminal tail of the diagonally opposite subunit, forming an anti-parallel beta sheet that constitutes part of the substrate binding site. The sulfonate group of isethionate is stabilized by a hydrogen bond network formed by the residues Y148, R195, Q244 and a water molecule. In addition, F249 from the diagonal subunit restrains the conformation of Y148 to further stabilize the orientation of the sulfonate group. Mutation of any of these four residues into alanine resulted in a complete loss of catalytic activity for isethionate oxidation. Biochemical investigations of the substrate scope of IsfD, and bioinformatics analysis of IsfD homologs, suggest that IsfD is related to the promiscuous 3-hydroxyacid dehydrogenases with diverse metabolic functions. Biochemical and structural investigation of sulfoacetaldehyde reductase from Klebsiella oxytoca.,Zhou Y, Wei Y, Lin L, Xu T, Ang EL, Zhao H, Yuchi Z, Zhang Y Biochem J. 2019 Feb 4. pii: BCJ20190005. doi: 10.1042/BCJ20190005. PMID:30718306 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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