1t4o: Difference between revisions

Line 1:

[[Image:1t4o.gif|left|200px]]<br /><applet load="1t4o" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1t4o.gif|left|200px]]<br /><applet load="1t4o" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1t4o, resolution 2.50Å" />

'''Crystal structure of rnt1p dsRBD'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1T4O OCA].

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==

Line 14:

[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Edwards, T.E.]]

[[Category: Edwards, T E.]]

[[Category: Godin, K.S.]]

[[Category: Godin, K S.]]

[[Category: Graille, M.]]

[[Category: Jr., M.Ares.]]

[[Category: Jr., M Ares.]]

[[Category: Leeper, T.C.]]

[[Category: Leeper, T C.]]

[[Category: Leulliot, N.]]

[[Category: Nagel, R.J.]]

[[Category: Nagel, R J.]]

[[Category: Quevillon-Cheruel, S.]]

[[Category: Rozenkrants, N.]]

[[Category: Sigurdsson, S.T.]]

[[Category: Sigurdsson, S T.]]

[[Category: Tilbeurgh, H.van.]]

[[Category: Tilbeurgh, H van.]]

[[Category: Varani, G.]]

[[Category: dsrbd]]

Line 30:

[[Category: rnt1p]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:50 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1t4o.gif|left|200px]]<br /><applet load="1t4o" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1t4o.gif|left|200px]]<br /><applet load="1t4o" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1t4o, resolution 2.50&Aring;" />
 '''Crystal structure of rnt1p dsRBD'''<br />
 ==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.
+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==
-T4O 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T4O OCA].
+T4O 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==
@@ Line 14: / Line 14: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Edwards, T.E.]]
+[[Category: Edwards, T E.]]
-[[Category: Godin, K.S.]]
+[[Category: Godin, K S.]]
 [[Category: Graille, M.]]
-[[Category: Jr., M.Ares.]]
+[[Category: Jr., M Ares.]]
-[[Category: Leeper, T.C.]]
+[[Category: Leeper, T C.]]
 [[Category: Leulliot, N.]]
-[[Category: Nagel, R.J.]]
+[[Category: Nagel, R J.]]
 [[Category: Quevillon-Cheruel, S.]]
 [[Category: Rozenkrants, N.]]
-[[Category: Sigurdsson, S.T.]]
+[[Category: Sigurdsson, S T.]]
-[[Category: Tilbeurgh, H.van.]]
+[[Category: Tilbeurgh, H van.]]
 [[Category: Varani, G.]]
 [[Category: dsrbd]]
@@ Line 30: / Line 30: @@
 [[Category: rnt1p]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:59:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:50 2008''