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Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.(BIOCHEMISTRY)(Author abstract)(Report)

Chakravarty, Anupam K. ; Smith, Paul ; Shuman, Stewart

Proceedings of the National Academy of Sciences of the United States, Dec 27, 2011, Vol.108(52), p.21034(6) [Tạp chí có phản biện]

ISSN: 0027-8424

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  • Nhan đề:
    Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.(BIOCHEMISTRY)(Author abstract)(Report)
  • Tác giả: Chakravarty, Anupam K. ; Smith, Paul ; Shuman, Stewart
  • Chủ đề: Phosphates -- Physiological Aspects ; Rna -- Physiological Aspects ; Atp -- Physiological Aspects ; Catalysis -- Research
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, Dec 27, 2011, Vol.108(52), p.21034(6)
  • Mô tả: RNA 3'-phosphate cyclase (RtcA) synthesizes RNA 2',3' cyclic phosphate ends via three steps: reaction with ATP to form a covalent RtcA-(histidinyl-N[epsilon])-AMP intermediate; transfer of adenylate to an RNA 3'-phosphate to form RNA(3')pp(5')A; and attack of the vicinal 02' on the 3'-phosphorus to form a 2',3' cyclic phosphate and release AMP. Here we report the crystal structures of RtcA x ATP, RtcA x ATP x [Mn.sup.2+], and RtcA x ATP x [Co.sup.2+] substrate complexes and an RtcA x AMP product complex. Together with the structures of RtcA apoenzyme and the covalent RtcA-AMP intermediate, they illuminate the mechanism of nucleotidyl transfer, especially the stereochemical transitions at the AMP phosphate, the critical role of the metal in orienting the PPz leaving group of ATP during step 1, and the protein conformational switches that accompany substrate binding and product release. The octahedral metal complex of RtcA x ATP x [Mn.sup.2+] includes nonbridging oxygens from each of the ATP phosphates, two waters, and Glu14 as the sole RtcA component, Whereas the RtcA adenylylation step is metal-catalyzed, the subsequent steps in the cyclization pathway are metal-independent, covalent catalysis | RNA modification doi/10.1073/pnas.1115560108
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

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