DC Field | Value | Language |
---|---|---|
dc.contributor.author | Seo, Pil-Won | - |
dc.contributor.author | Hofmann, Andreas | - |
dc.contributor.author | Kim, Jun-Ha | - |
dc.contributor.author | Hwangbo, Seung-A | - |
dc.contributor.author | Kim, Jun-Hong | - |
dc.contributor.author | Kim, Ji-Won | - |
dc.contributor.author | Huynh, Thi Yen Ly | - |
dc.contributor.author | Choy, Hyon E. | - |
dc.contributor.author | Kim, Soo-Jung | - |
dc.contributor.author | Lee, Jimin | - |
dc.contributor.author | Lee, Jie-Oh | - |
dc.contributor.author | Jin, Kyeong Sik | - |
dc.contributor.author | Park, Suk-Youl | - |
dc.contributor.author | Kim, Jeong-Sun | - |
dc.date.accessioned | 2022-04-14T08:40:06Z | - |
dc.date.available | 2022-04-14T08:40:06Z | - |
dc.date.created | 2022-04-05 | - |
dc.date.issued | 2022-05 | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/112461 | - |
dc.description.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 | - |
dc.language | English | - |
dc.publisher | Elsevier BV | - |
dc.relation.isPartOf | International Journal of Biological Macromolecules | - |
dc.title | Structural features of a minimal intact methyltransferase of a type I restriction-modification system | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2022.03.115 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | International Journal of Biological Macromolecules, v.208, pp.381 - 389 | - |
dc.identifier.wosid | 000793588500007 | - |
dc.citation.endPage | 389 | - |
dc.citation.startPage | 381 | - |
dc.citation.title | International Journal of Biological Macromolecules | - |
dc.citation.volume | 208 | - |
dc.contributor.affiliatedAuthor | Hwangbo, Seung-A | - |
dc.contributor.affiliatedAuthor | Lee, Jimin | - |
dc.contributor.affiliatedAuthor | Lee, Jie-Oh | - |
dc.contributor.affiliatedAuthor | Jin, Kyeong Sik | - |
dc.contributor.affiliatedAuthor | Park, Suk-Youl | - |
dc.identifier.scopusid | 2-s2.0-85127029986 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | ARDA ANTIRESTRICTION PROTEIN | - |
dc.subject.keywordPlus | MODIFICATION ENZYME | - |
dc.subject.keywordPlus | BACTERIOPHAGE T7 | - |
dc.subject.keywordPlus | DNA RESTRICTION | - |
dc.subject.keywordPlus | PLASMID PKM101 | - |
dc.subject.keywordPlus | SUBUNIT | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | MIMICRY | - |
dc.subject.keywordPlus | MODEL | - |
dc.subject.keywordAuthor | Methyltransferase | - |
dc.subject.keywordAuthor | Ocr | - |
dc.subject.keywordAuthor | Type I restriction-modification system | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Applied | - |
dc.relation.journalWebOfScienceCategory | Polymer Science | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Polymer Science | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
library@postech.ac.kr Tel: 054-279-2548
Copyrights © by 2017 Pohang University of Science ad Technology All right reserved.