7qx8

Crystal structure of serine hydroxymethyltransferase, isoform 7 from Arabidopsis thaliana (SHM7)

spinqualitylabelsall models 7qx8, resolution 2.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qx8 is a 12 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.74Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLYC7_ARATH Catalyzes the interconversion of serine and glycine. Publication Abstract from PubMed Serine hydroxymethyltransferase (SHM) is one of the hallmarks of one-carbon metabolism. In plants, isoforms of SHM participate in photorespiration and/or transfer the one-carbon unit from L-serine to tetrahydrofolate (THF), hence producing 5,10-CH2-THF that is needed, e.g., for biosynthesis of methionine, thymidylate, and purines. These links highlight the importance of SHM activity in DNA biogenesis, its epigenetic methylations, and in stress responses. Plant genomes encode several SHM isoforms that localize to cytosol, mitochondria, plastids, and nucleus. In this work, we present a thorough functional and structural characterization of all seven SHM isoforms from Arabidopsis thaliana (AtSHM1-7). In particular, we analyzed tissue-specific expression profiles of the AtSHM genes. We also compared catalytic properties of the active AtSHM1-4 in terms of catalytic efficiency in both directions and inhibition by the THF substrate. Despite numerous attempts to rescue the SHM activity of AtSHM5-7, we failed, which points towards different physiological functions of these isoforms. Comparative analysis of experimental and predicted three-dimensional structures of AtSHM1-7 proteins indicated differences in regions that surround the entrance to the active site cavity. Arabidopsis thaliana serine hydroxymethyltransferases: functions, structures, and perspectives.,Nogues I, Sekula B, Angelaccio S, Grzechowiak M, Tramonti A, Contestabile R, Ruszkowski M Plant Physiol Biochem. 2022 Jul 31;187:37-49. doi: 10.1016/j.plaphy.2022.07.025. PMID:35947902 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine hydroxymethyltransferase 3D structures

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