9vsm | pdb_00009vsm

Crystal structure of cystathionine gamma-synthase from Lactobacillus plantarum complexed with the cystathionine-bound external aldimine

spinqualitylabelsall models 9vsm, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9vsm is a 4 chain structure with sequence from Lactiplantibacillus plantarum WCFS1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: E9U Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Cystathionine gamma-synthase (CGS) and cystathionine gamma-lyase (CGL) have highly similar amino acid sequences. CGS catalyzes the generation of cystathionine from acylated l-homoserine and l-cysteine, whereas CGL catalyzes the decomposition of cystathionine to produce l-cysteine. Lactobacillus plantarum is a unique bacterium containing two open reading frames of CGL/CGS enzymes in its genome. Structural studies of LpCGS and LpCGL may provide insights into their reaction specificities. In the present study, we elucidated the structure and enzymatic function of LpCGS. We found that LpCGS has substrate specificity toward acetylated rather than succinylated l-homoserine. LpCGS has the characteristic residues E55 and V232 in the substrate-binding pocket, which synergistically confer substrate specificity toward acetylated l-homoserine. These results may facilitate the development of inhibitors of l-methionine and l-cysteine biosynthetic pathways. Structural insight into the substrate specificity of cystathionine gamma-synthase from Lactobacillus plantarum.,Matoba Y, Oda K, Ohtani M, Mende Y, Noda K FEBS Lett. 2026 Jan 21. doi: 10.1002/1873-3468.70276. PMID:41562399 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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