1T4O

Crystal structure of rnt1p dsRBD

Summary for 1T4O

• Entry DOI: 10.2210/pdb1t4o/pdb
• Related: 1T4N
• Descriptor: Ribonuclease III (2 entities in total)
• Functional Keywords: rnt1p, dsrbd, rna-binding, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 26414.56

Authors

Leulliot, N.,Quevillon-Cheruel, S.,Graille, M.,van Tilbeurgh, H.,Leeper, T.C.,Godin, K.S.,Edwards, T.E.,Sigurdsson, S.T.,Rozenkrants, N.,Nagel, R.J.,Ares Jr., M.,Varani, G. (deposition date: 2004-04-30, release date: 2004-06-22, Last modification date: 2023-08-23)

Primary citation

Leulliot, N.,Quevillon-Cheruel, S.,Graille, M.,Van Tilbeurgh, H.,Leeper, T.C.,Godin, K.S.,Edwards, T.E.,Sigurdsson, S.T.,Rozenkrants, N.,Nagel, R.J.,Ares, M.,Varani, G.
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III
Embo J., 23:2468-2477, 2004

PubMed Abstract: 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.

PubMed: 15192703
DOI: 10.1038/sj.emboj.7600260

Experimental method

X-RAY DIFFRACTION (2.5 Å)