7eew | pdb_00007eew

Crystal structure of the intact MTase from Vibrio vulnificus YJ016 in complex with the DNA-mimicking Ocr protein and the S-adenosyl-L-homocysteine (SAH)

spinqualitylabelsall models 7eew, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7eew is a 2 chain structure with sequence from Escherichia phage T7 and Vibrio vulnificus YJ016. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.896Å Ligands: SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7MJG0_VIBVY Publication Abstract from PubMed Type I restriction-modification enzymes are oligomeric proteins composed of methylation (M), DNA sequence-recognition (S), and restriction (R) subunits. The different bipartite DNA sequences of 2-4 consecutive bases are recognized by two discerned target recognition domains (TRDs) located at the two-helix bundle of the two conserved regions (CRs). Two M-subunits and a single S-subunit form an oligomeric protein that functions as a methyltransferase (M(2)S(1) MTase). Here, we present the crystal structure of the intact MTase from Vibrio vulnificus YJ016 in complex with the DNA-mimicking Ocr protein and the S-adenosyl-L-homocysteine (SAH). This MTase includes the M-domain with a helix tail (M-tail helix) and the S(1/2)-domain of a TRD and a CR alpha-helix. The Ocr binds to the cleft of the TRD surface and SAH is located in the pocket within the M-domain. The solution- and negative-staining electron microscopy-based reconstructed (M(1)S(1/2))(2) structure reveals a symmetric (S(1/2))(2) assembly using two CR-helices and two M-tail helices as a pivot, which is plausible for recognizing two DNA regions of same sequence. The conformational flexibility of the minimal M(1)S(1/2) MTase dimer indicates a particular state resembling the structure of M(2)S(1) MTases. Structural features of a minimal intact methyltransferase of a type I restriction-modification system.,Seo PW, Hofmann A, Kim JH, Hwangbo SA, Kim JH, Kim JW, Huynh TYL, Choy HE, Kim SJ, Lee J, Lee JO, Jin KS, Park SY, Kim JS Int J Biol Macromol. 2022 May 31;208:381-389. doi: , 10.1016/j.ijbiomac.2022.03.115. Epub 2022 Mar 23. PMID:35337914 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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