6ltv | pdb_00006ltv

Crystal Structure of I122A/I330A variant of S-adenosylmethionine synthetase from Cryptosporidium hominis in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)

spinqualitylabelsall models 6ltv, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ltv is a 2 chain structure with sequence from Cryptosporidium hominis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Ligands: 3PO, EU9, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0S4TKQ5_CRYHO Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] Publication Abstract from PubMed Methylation and demethylation of DNA, RNA and proteins has emerged as a major regulatory mechanism. Studying the function of these modifications would benefit from tools for their site-specific inhibition and timed removal. S -Adenosyl-L-methionine (AdoMet) analogs in combination with methyltransferases (MTases) have proven useful to map or block and release MTase target sites, however their enzymatic generation has been limited to aliphatic groups at the sulfur atom. We engineered a SAM synthetase from Cryptosporidium hominis (PC-ChMAT) for efficient generation of AdoMet analogs with photocaging groups that are not accepted by any WT MAT reported to date. The crystal structure of PC-ChMAT at 1.87 A revealed how the photocaged AdoMet analog is accommodated and guided engineering of a thermostable MAT from Methanocaldococcus jannaschii . PC-MATs were compatible with DNA- and RNA MTases, enabling sequence-specific modification ("writing") of plasmid DNA and light-triggered removal ("erasing"). Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions.,Michailidou F, Klocker N, Cornelissen N, Singh RK, Peters A, Ovcharenko A, Kummel D, Rentmeister A Angew Chem Int Ed Engl. 2020 Oct 5. doi: 10.1002/anie.202012623. PMID:33017502 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also S-adenosylmethionine synthetase 3D structures

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