Structural basis for 16S ribosomal RNA cleavage by the cytotoxic domain of colicin E3.
The toxin colicin E3 targets the 30S subunit of bacterial ribosomes and cleaves a phosphodiester bond in the decoding center. We present the crystal structure of the 70S ribosome in complex with the cytotoxic domain of colicin E3 (E3-rRNase). The structure reveals how the rRNase domain of colicin bi...
المؤلفون الرئيسيون: | Ng, C, Lang, K, Meenan, N, Sharma, A, Kelley, A, Kleanthous, K, Ramakrishnan, V |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2010
|
مواد مشابهة
-
Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes.
حسب: Lancaster, L, وآخرون
منشور في: (2008) -
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
حسب: Keeble, A, وآخرون
منشور في: (2008) -
Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation.
حسب: Bonsor, D, وآخرون
منشور في: (2008) -
The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes.
حسب: Keeble, A, وآخرون
منشور في: (2005) -
Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3.
حسب: Walker, D, وآخرون
منشور في: (2004)