1t4o
From Proteopedia
(New page: 200px<br /><applet load="1t4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t4o, resolution 2.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1t4o.gif|left|200px]]<br /><applet load="1t4o" size=" | + | [[Image:1t4o.gif|left|200px]]<br /><applet load="1t4o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t4o, resolution 2.50Å" /> | caption="1t4o, resolution 2.50Å" /> | ||
'''Crystal structure of rnt1p dsRBD'''<br /> | '''Crystal structure of rnt1p dsRBD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rnt1 endoribonuclease, the yeast homolog of RNAse III, plays an important | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1T4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] Full crystallographic information is available from [http:// | + | 1T4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Edwards, T | + | [[Category: Edwards, T E.]] |
| - | [[Category: Godin, K | + | [[Category: Godin, K S.]] |
[[Category: Graille, M.]] | [[Category: Graille, M.]] | ||
| - | [[Category: Jr., M | + | [[Category: Jr., M Ares.]] |
| - | [[Category: Leeper, T | + | [[Category: Leeper, T C.]] |
[[Category: Leulliot, N.]] | [[Category: Leulliot, N.]] | ||
| - | [[Category: Nagel, R | + | [[Category: Nagel, R J.]] |
[[Category: Quevillon-Cheruel, S.]] | [[Category: Quevillon-Cheruel, S.]] | ||
[[Category: Rozenkrants, N.]] | [[Category: Rozenkrants, N.]] | ||
| - | [[Category: Sigurdsson, S | + | [[Category: Sigurdsson, S T.]] |
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H van.]] |
[[Category: Varani, G.]] | [[Category: Varani, G.]] | ||
[[Category: dsrbd]] | [[Category: dsrbd]] | ||
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[[Category: rnt1p]] | [[Category: rnt1p]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:50 2008'' |
Revision as of 13:09, 21 February 2008
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Crystal structure of rnt1p dsRBD
Overview
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.
About this Structure
1T4O is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Ribonuclease III, with EC number 3.1.26.3 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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