Structural features of a minimal intact methyltransferase of a type I restriction-modification system
SCIE
SCOPUS
- Title
- Structural features of a minimal intact methyltransferase of a type I restriction-modification system
- Authors
- Seo, Pil-Won; Hofmann, Andreas; Kim, Jun-Ha; Hwangbo, Seung-A; Kim, Jun-Hong; Kim, Ji-Won; Huynh, Thi Yen Ly; Choy, Hyon E.; Kim, Soo-Jung; Lee, Jimin; Lee, Jie-Oh; Jin, Kyeong Sik; Park, Suk-Youl; Kim, Jeong-Sun
- Date Issued
- 2022-05
- Publisher
- Elsevier BV
- Abstract
- 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 (M2S1 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 S1/2-domain of a TRD and a CR α-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 (M1S1/2)2 structure reveals a symmetric (S1/2)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 M1S1/2 MTase dimer indicates a particular state resembling the structure of M2S1 MTases. © 2022
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/112461
- DOI
- 10.1016/j.ijbiomac.2022.03.115
- ISSN
- 0141-8130
- Article Type
- Article
- Citation
- International Journal of Biological Macromolecules, vol. 208, page. 381 - 389, 2022-05
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