期刊
SCIENCE
卷 320, 期 5872, 页码 77-82出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1153803
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资金
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [GM50313, R01 GM050313] Funding Source: Medline
- NLM NIH HHS [T15 LM07056] Funding Source: Medline
Group II introns are self- splicing ribozymes that catalyze their own excision from precursor transcripts and insertion into new genetic locations. Here we report the crystal structure of an intact, self- spliced group II intron from Oceanobacillus iheyensis at 3.1 angstrom resolution. An extensive network of tertiary interactions facilitates the ordered packing of intron subdomains around a ribozyme core that includes catalytic domain V. The bulge of domain V adopts an unusual helical structure that is located adjacent to a major groove triple helix ( catalytic triplex). The bulge and catalytic triplex jointly coordinate two divalent metal ions in a configuration that is consistent with a two- metal ion mechanism for catalysis. Structural and functional analogies support the hypothesis that group II introns and the spliceosome share a common ancestor.
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