Literature DB >> 12005430

Structure and dynamics of the anticodon arm binding domain of Bacillus stearothermophilus Tyrosyl-tRNA synthetase.

J Iñaki Guijarro1, Alessandro Pintar, Ada Prochnicka-Chalufour, Valérie Guez, Bernard Gilquin, Hugues Bedouelle, Muriel Delepierre.   

Abstract

The structure of a recombinant protein, TyrRS(delta4), corresponding to the anticodon arm binding domain of Bacillus stearothermophilus tyrosyl-tRNA synthetase, has been solved, and its dynamics have been studied by nuclear magnetic resonance (NMR). It is the first structure described for such a domain of a tyrosyl-tRNA synthetase. It consists of a five-stranded beta sheet, packed against two alpha helices on one side and one alpha helix on the other side. A large part of the domain is structurally similar to other functionally unrelated RNA binding proteins. The basic residues known to be essential for tRNA binding and charging are exposed to the solvent on the same face of the molecule. The structure of TyrRS(delta4), together with previous mutagenesis data, allows one to delineate the region of interaction with tRNATyr.

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Year:  2002        PMID： 12005430     DOI： 10.1016/s0969-2126(02)00699-8

Source DB:  PubMed          Journal:  Structure        ISSN： 0969-2126            Impact factor:   5.006


  8 in total

1.  Identification and evolution of fungal mitochondrial tyrosyl-tRNA synthetases with group I intron splicing activity.

Authors:  Paul J Paukstelis; Alan M Lambowitz
Journal:  Proc Natl Acad Sci U S A       Date:  2008-04-14       Impact factor: 11.205

2.  Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module.

Authors:  Wei Yan; Qing Ye; Min Tan; Xi Chen; Gilbert Eriani; En-Duo Wang
Journal:  J Biol Chem       Date:  2015-03-27       Impact factor: 5.157

3.  3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample.

Authors:  Anna Krejcirikova; Vitali Tugarinov
Journal:  J Biomol NMR       Date:  2012-09-08       Impact factor: 2.835

4.  NMR Structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.

Authors:  Paul J Paukstelis; Nandini Chari; Alan M Lambowitz; David Hoffman
Journal:  Biochemistry       Date:  2011-04-12       Impact factor: 3.162

5.  A novel homozygous YARS2 mutation causes severe myopathy, lactic acidosis, and sideroblastic anemia 2.

Authors:  Junya Nakajima; Tuba F Eminoglu; Goksel Vatansever; Mitsuko Nakashima; Yoshinori Tsurusaki; Hirotomo Saitsu; Hisashi Kawashima; Naomichi Matsumoto; Noriko Miyake
Journal:  J Hum Genet       Date:  2014-01-16       Impact factor: 3.172

6.  Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.

Authors:  Tamara Frembgen-Kesner; Casey T Andrews; Shuxiang Li; Nguyet Anh Ngo; Scott A Shubert; Aakash Jain; Oluwatoni J Olayiwola; Mitch R Weishaar; Adrian H Elcock
Journal:  J Chem Theory Comput       Date:  2015-04-30       Impact factor: 6.006

7.  Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition.

Authors:  Anna Yaremchuk; Ivan Kriklivyi; Michael Tukalo; Stephen Cusack
Journal:  EMBO J       Date:  2002-07-15       Impact factor: 11.598

8.  Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms.

Authors:  Masaru Tsunoda; Yoshio Kusakabe; Nobutada Tanaka; Satoshi Ohno; Masashi Nakamura; Toshiya Senda; Tomohisa Moriguchi; Norio Asai; Mitsuo Sekine; Takashi Yokogawa; Kazuya Nishikawa; Kazuo T Nakamura
Journal:  Nucleic Acids Res       Date:  2007-06-18       Impact factor: 16.971
  8 in total

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