1QHK

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

Summary for 1QHK

• Entry DOI: 10.2210/pdb1qhk/pdb
• NMR Information: BMRB: 4424
• Descriptor: PROTEIN (RIBONUCLEASE HI) (1 entity in total)
• Functional Keywords: ribonuclease hi n-terminal domain, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 5380.94

Authors

Evans, S.P.,Bycroft, M. (deposition date: 1999-05-17, release date: 1999-08-31, Last modification date: 2023-12-27)

Primary citation

Evans, S.P.,Bycroft, M.
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.
J.Mol.Biol., 291:661-669, 1999

PubMed Abstract: 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.

PubMed: 10448044
DOI: 10.1006/jmbi.1999.2971

Experimental method

SOLUTION NMR