1un6
From Proteopedia
THE CRYSTAL STRUCTURE OF A ZINC FINGER - RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION
Structural highlights
FunctionTF3A_XENLA Acts as both a positive transcription factor for 5S RNA genes and a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedZinc-finger proteins of the classical Cys2His2 type are the most frequently used class of transcription factor and account for about 3% of genes in the human genome. The zinc-finger motif was discovered during biochemical studies on the transcription factor TFIIIA, which regulates the 5S ribosomal RNA genes of Xenopus laevis. Zinc-fingers mostly interact with DNA, but TFIIIA binds not only specifically to the promoter DNA, but also to 5S RNA itself. Increasing evidence indicates that zinc-fingers are more widely used to recognize RNA. There have been numerous structural studies on DNA binding, but none on RNA binding by zinc-finger proteins. Here we report the crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete nine-finger TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger binding, both of which differ from that in common use for DNA: first, the zinc-fingers interact with the backbone of a double helix; and second, the zinc-fingers specifically recognize individual bases positioned for access in otherwise intricately folded 'loop' regions of the RNA. Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition.,Lu D, Searles MA, Klug A Nature. 2003 Nov 6;426(6962):96-100. PMID:14603324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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