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December 7, 2022Protein ScienceOpen Access

Ribonuclease T2 represents a distinct circularly permutated version of the BECR RNases

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Authors

HLHuan LiBeijing Institute of Fashion TechnologyTSTheresa SchneiderUniversitätsklinikum WürzburgYTYongjun TanUniversity of Missouri–St. Louis

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Implication

Identifies RNase T2 as a unique version of BECR RNases, suggesting novel evolutionary insights.

Key Points

  • The aim is to explore the homologous relationships between ribonuclease T2 and BECR RNases.
  • Utilized reverse circular permutation process for ancestral reconstruction of RNase T2.
  • Applied structural modeling using AlphaFold2 for comparison.
  • Investigated catalytic site configurations of RNases.
  • Demonstrated that RNase T2 reflects a circularly permutated BECR fold RNase with similar catalytic configurations.
  • Identified structural similarity between RNase T2 and typical BECR RNases through advanced modeling techniques.
  • Highlighted RNase T2's origins linked to bacterial toxin systems.

Cite This Study

Li et al. (2022) studied this question.

synapsesocial.com/papers/6a20ebe6e2d1a39857ecc715https://doi.org/10.1002/pro.4531
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