7lt5 | pdb_00007lt5

CamA Adenine Methyltransferase Complexed to Cognate Substrate DNA and Cofactor SAH

spinqualitylabelsall models 7lt5, resolution 2.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7lt5 is a 9 chain structure with sequence from Clostridioides difficile and Clostridioides difficile 630. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.54Å Ligands: EDO, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q183J3_CLOD6 Publication Abstract from PubMed Clostridioides difficile infections are an urgent medical problem. The newly discovered C. difficile adenine methyltransferase A (CamA) is specified by all C. difficile genomes sequenced to date (>300), but is rare among other bacteria. CamA is an orphan methyltransferase, unassociated with a restriction endonuclease. CamA-mediated methylation at CAAAAA is required for normal sporulation, biofilm formation, and intestinal colonization by C. difficile. We characterized CamA kinetic parameters, and determined its structure bound to DNA containing the recognition sequence. CamA contains an N-terminal domain for catalyzing methyl transfer, and a C-terminal DNA recognition domain. Major and minor groove DNA contacts in the recognition site involve base-specific hydrogen bonds, van der Waals contacts and the Watson-Crick pairing of a rearranged A:T base pair. These provide sufficient sequence discrimination to ensure high specificity. Finally, the surprisingly weak binding of the methyl donor S-adenosyl-L-methionine (SAM) might provide avenues for inhibiting CamA activity using SAM analogs. Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix.,Zhou J, Horton JR, Blumenthal RM, Zhang X, Cheng X Nat Commun. 2021 Jun 8;12(1):3436. doi: 10.1038/s41467-021-23693-w. PMID:34103525 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA methyltransferase 3D structures

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