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Structural basis for methyl transfer by a radical SAM enzyme.(REPORTS)(S-adenosyl-L-methionine)(Author abstract)(Report)

Boal, Amie K. ; Grove, Tyler L. ; Mclaughlin, Monica I. ; Yennawar, Neela H. ; Booker, Squire J. ; Rosenzweig, Amy C.

Science, May 27, 2011, Vol.332(6033), p.1089(4) [Tạp chí có phản biện]

ISSN: 0036-8075

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  • Nhan đề:
    Structural basis for methyl transfer by a radical SAM enzyme.(REPORTS)(S-adenosyl-L-methionine)(Author abstract)(Report)
  • Tác giả: Boal, Amie K. ; Grove, Tyler L. ; Mclaughlin, Monica I. ; Yennawar, Neela H. ; Booker, Squire J. ; Rosenzweig, Amy C.
  • Chủ đề: Methylation -- Physiological Aspects ; S-adenosylmethionine -- Properties
  • Là 1 phần của: Science, May 27, 2011, Vol.332(6033), p.1089(4)
  • Mô tả: The radical S-adenosyl-L-methionine (SAM) enzymes RImN and Cfr rnethytate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RImN [Cys.sup.355]) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. Crystal structures of RlmN and RlmN with SAM show that a single moLecuLe of SAM coordinates the [4Fe-4S] duster. Residue [Cys.sup.355] is S-methylated and located proxirnal to the SAM rnethyl group, suggesting the SAM that is involved in the initial methyl transfer binds at the same site. Thus, RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site. 10.1126/science.1205358
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0036-8075

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