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pro vyhledávání: '"Charmaine Hoang"'
Autor:
Junjun Chen, Eugene G. Mueller, Christopher S. Hamilton, Charmaine Hoang, Caroline A. Vizthum, Jason M. Kandel, Adrian R. Ferré-D'Amaré
Publikováno v:
Molecular Cell. 24(4):535-545
Summary RluA is a dual-specificity enzyme responsible for pseudouridylating 23S rRNA and several tRNAs. The 2.05 A resolution structure of RluA bound to a substrate RNA comprising the anticodon stem loop of tRNA Phe reveals that enzyme binding induce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b9b15a93fbba92d9d95fffc1cd53e1d
Publikováno v:
Protein science : a publication of the Protein Society. 14(8)
The pseudouridine synthase TruB is responsible for the universally conserved post-transcriptional modification of residue 55 of elongator tRNAs. In addition to the active site, the “thumb,” a peripheral domain unique to the TruB family of enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01211893adad4aa0a402383b4b24e052
https://pubmed.ncbi.nlm.nih.gov/15987897
https://pubmed.ncbi.nlm.nih.gov/15987897
Publikováno v:
RNA (New York, N.Y.). 10(7)
The pseudouridine (Ψ) synthases Pus7p and TruD define a family of RNA-modifying enzymes with no sequence similarity to previously characterized Ψ synthases. The 2.2 Å resolution structure of Escherichia coli TruD reveals a U-shaped molecule with a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b89f0af633dc0b066350474457b8dd1a
https://pubmed.ncbi.nlm.nih.gov/15208439
https://pubmed.ncbi.nlm.nih.gov/15208439