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1qhk

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1qhk

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N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9

Overview

In addition to the conserved and well-defined RNase H domain, eukaryotic, RNases HI possess either one or two copies of a small N-terminal domain., The solution structure of one of the N-terminal domains from Saccharomyces, cerevisiae RNase HI, determined using NMR spectroscopy, is presented. The, 46 residue motif comprises a three-stranded antiparallel beta-sheet and, two short alpha-helices which pack onto opposite faces of the beta-sheet., Conserved residues involved in packing the alpha-helices onto the, beta-sheet form the hydrophobic core of the domain. Three highly conserved, and solvent exposed residues are implicated in RNA binding, W22, K38 and, K39. The beta-beta-alpha-beta-alpha topology of the domain differs from, the structures of known RNA binding domains such as the double-stranded, RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP, motif. However, structural similarities exist between this domain and the, N-terminal domain of ribosomal protein L9 which binds to 23 S ribosomal, RNA.

About this Structure

1QHK is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Ribonuclease H, with EC number 3.1.26.4 Full crystallographic information is available from OCA.

Reference

NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9., Evans SP, Bycroft M, J Mol Biol. 1999 Aug 20;291(3):661-9. PMID:10448044

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