4wxb

Crystal Structure of Serine Hydroxymethyltransferase from Streptococcus thermophilus

spinqualitylabelsall models 4wxb, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wxb is a 4 chain structure with sequence from Streptococcus thermophilus CNRZ1066. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: CAC, CIT, GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLYA_STRT1 Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Publication Abstract from PubMed alpha,alpha-Disubstituted alpha-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5'-phosphate (PLP)-dependent L-serine hydroxymethyltransferase from Streptococcus thermophilus (SHMTSth ; EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of alpha,alpha-dialkyl-alpha-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids D-Ala and D-Ser to a wide acceptor scope catalyzed by the minimalist SHMTSth Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMTSth Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors. Engineered L-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of alpha,alpha-Dialkyl-alpha-Amino Acids.,Hernandez K, Zelen I, Petrillo G, Uson I, Wandtke CM, Bujons J, Joglar J, Parella T, Clapes P Angew Chem Int Ed Engl. 2015 Jan 21. doi: 10.1002/anie.201411484. PMID:25611820 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine hydroxymethyltransferase 3D structures

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