1t4o

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{{STRUCTURE_1t4o| PDB=1t4o | SCENE= }}
{{STRUCTURE_1t4o| PDB=1t4o | SCENE= }}
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'''Crystal structure of rnt1p dsRBD'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15192703 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15192703}}
==About this Structure==
==About this Structure==
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[[Category: Rna-binding]]
[[Category: Rna-binding]]
[[Category: Rnt1p]]
[[Category: Rnt1p]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:31:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:57:04 2008''

Revision as of 12:57, 28 July 2008

Image:1t4o.png

Template:STRUCTURE 1t4o

Crystal structure of rnt1p dsRBD

Template:ABSTRACT PUBMED 15192703

About this Structure

1T4O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III., Leulliot N, Quevillon-Cheruel S, Graille M, van Tilbeurgh H, Leeper TC, Godin KS, Edwards TE, Sigurdsson ST, Rozenkrants N, Nagel RJ, Ares M, Varani G, EMBO J. 2004 Jul 7;23(13):2468-77. Epub 2004 Jun 10. PMID:15192703

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