1t4n

<StructureSection load='1t4n' size='340' side='right'caption='[[1t4n]], [[NMR_Ensembles_of_Models | 51 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1t4n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4N FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t4o|1t4o]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNT1, YMR239C, YM9408.01C, YM9959.21 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] </span></td></tr>

[[https://www.uniprot.org/uniprot/RNT1_YEAST RNT1_YEAST]] DsRNA-specific nuclease that cleaves eukaryotic pre-ribosomal RNA at the U3 snoRNP-dependent A0 site in the 5'-external transcribed spacer (ETS) and in the 3'-ETS. In vitro, cleaves synthetic 5'-ETS RNA A0 site in the absence of snoRNA or other factors. Has an essential growth function in addition to pre-rRNA processing.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15192703</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1t4n" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Ribonuclease III]]

[[Category: Ares, M]]

[[Category: Edwards, T E]]

[[Category: Godin, K S]]

[[Category: Graille, M]]

[[Category: Leeper, T C]]

[[Category: Leulliot, N]]

[[Category: Nagel, R J]]

[[Category: Quevillon-Cheruel, S]]

[[Category: Rozenkrants, N]]

[[Category: Sigurdsson, S T]]

[[Category: Tilbeurgh, H van]]

[[Category: Varani, G]]

[[Category: Dsrbd]]

[[Category: Rna-binding]]