期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 15, 期 1, 页码 103-105出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1327
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资金
- NHLBI NIH HHS [5T32HL007675-19, T32 HL007675] Funding Source: Medline
- NIAMS NIH HHS [R01 AR041480-12, AR-41480, R01 AR041480-14, R01 AR041480, R01 AR041480-13] Funding Source: Medline
- NIBIB NIH HHS [R01 EB002060-24, EB-002060, R01 EB002060-23, R01 EB002060-25, R01 EB002060] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [T32HL007675] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES [R01AR041480] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R01EB002060] Funding Source: NIH RePORTER
The cocrystal structure of the PP7 bacteriophage coat protein in complex with its translational operator identifies a distinct mode of sequence-specific RNA recognition when compared to the well-characterized MS2 coat protein-RNA complex. The structure reveals the molecular basis of the PP7 coat protein's ability to selectively bind its cognate RNA, and it demonstrates that the conserved beta-sheet surface is a flexible architecture that can evolve to recognize diverse RNA hairpins.
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