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Literature DB >> 6287278

Specific protein-nucleic acid recognition in ribonuclease T1-2'-guanylic acid complex: an X-ray study.

Abstract

RNase T1 is folded into an alpha-helix of 4.5 turns, covered by a four-strand antiparallel beta-sheet. Specific recognition of 2'-guanylic acid arises from hydrogen bonding between main chain peptide groups and the O-6 and N-1-H of guanine, as well as from stacking of Tyr 45 on guanine. At the active site, Glu 58, His 92 and Arg 77 are involved in phosphodiester hydrolysis.

Entities: Chemical Gene

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Year: 1982 PMID： 6287278 DOI： 10.1038/299027a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

35 in total

1. Contribution of active site residues to the activity and thermal stability of ribonuclease Sa.

Authors: Gennady I Yakovlev; Vladimir A Mitkevich; Kevin L Shaw; Saul Trevino; Stephanie Newsom; C Nick Pace; Alexander A Makarov
Journal: Protein Sci Date: 2003-10 Impact factor: 6.725

2. Tertiary structure of RNase Pch1 predicted from the model structure of RNase Ms and the crystal structure of RNase T1. Comparison among the model structures--testing the limits of modelling by homology.

Authors: R Floegel; P Zielenkiewicz; W Saenger
Journal: Eur Biophys J Date: 1990 Impact factor: 1.733

3. Anisotropy decays of single tryptophan proteins measured by GHz frequency-domain fluorometry with collisional quenching.

Authors: J R Lakowicz; I Gryczynski; H Szmacinski; H Cherek; N Joshi
Journal: Eur Biophys J Date: 1991 Impact factor: 1.733

Specific protein-nucleic acid recognition in ribonuclease T1-2'-guanylic acid complex: an X-ray study.

1. Contribution of active site residues to the activity and thermal stability of ribonuclease Sa.

2. Tertiary structure of RNase Pch1 predicted from the model structure of RNase Ms and the crystal structure of RNase T1. Comparison among the model structures--testing the limits of modelling by homology.

3. Anisotropy decays of single tryptophan proteins measured by GHz frequency-domain fluorometry with collisional quenching.

4. Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae.

5. Conformational heterogeneity in the Salmonella typhimurium pyrC and pyrD leader mRNAs produced in vivo.

6. A thermodynamic coupling mechanism for GroEL-mediated unfolding.

7. Are turns required for the folding of ribonuclease T1?

8. The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules.

9. Kinetics of tryptic hydrolysis of the arginine-valine bond in folded and unfolded ribonuclease T1.

10. A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1.