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| {{STRUCTURE_1t4o| PDB=1t4o | SCENE= }} | | {{STRUCTURE_1t4o| PDB=1t4o | SCENE= }} |
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| '''Crystal structure of rnt1p dsRBD'''
| | ===Crystal structure of rnt1p dsRBD=== |
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| ==Overview==
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| Rnt1 endoribonuclease, the yeast homolog of RNAse III, plays an important role in the maturation of a diverse set of RNAs. The enzymatic activity requires a conserved catalytic domain, while RNA binding requires the double-stranded RNA-binding domain (dsRBD) at the C-terminus of the protein. While bacterial RNAse III enzymes cleave double-stranded RNA, Rnt1p specifically cleaves RNAs that possess short irregular stem-loops containing 12-14 base pairs interrupted by internal loops and bulges and capped by conserved AGNN tetraloops. Consistent with this substrate specificity, the isolated Rnt1p dsRBD and the 30-40 amino acids that follow bind to AGNN-containing stem-loops preferentially in vitro. In order to understand how Rnt1p recognizes its cognate processing sites, we have defined its minimal RNA-binding domain and determined its structure by solution NMR spectroscopy and X-ray crystallography. We observe a new carboxy-terminal helix following a canonical dsRBD structure. Removal of this helix reduces binding to Rnt1p substrates. The results suggest that this helix allows the Rnt1p dsRBD to bind to short RNA stem-loops by modulating the conformation of helix alpha1, a key RNA-recognition element of the dsRBD.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15192703}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15192703 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15192703}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rna-binding]] | | [[Category: Rna-binding]] |
| [[Category: Rnt1p]] | | [[Category: Rnt1p]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:31:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:57:04 2008'' |
