Structural similarities in the noncatalytic domains of phenylalanyl‐tRNA and biotin synthetases
- 1 November 1995
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 4 (11) , 2429-2432
- https://doi.org/10.1002/pro.5560041122
Abstract
Detailed comparison between the structures of the Escherichia coli biotin synthetase/repressor protein (BirA) and the recently solved Thermus thermophilus phenylalanyl‐tRNA synthetase (PheRS) reveals significant similarities outside their respective catalytic domains. These comprise a DNA‐binding α+β domain and an Src‐homology 3 (SH3)‐like domain that were observed in both enzymes. This similarity provides a novel example in which all domains of one multidomain protein appear to be constituents of the other multidomain protein and supports a concept of a common ancestor for two different synthetase families.Keywords
This publication has 20 references indexed in Scilit:
- Structure of phenylalanyl-tRNA synthetase from Thermus thermophilusNature Structural & Molecular Biology, 1995
- The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coliStructure, 1995
- A tale of two synthetasesNature Structural & Molecular Biology, 1994
- Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5Nature, 1993
- Structural similarity of DNA-binding domains of bacteriophage repressors and the globin coreCurrent Biology, 1993
- DNA recognition by the helix-turn-helix motifCurrent Opinion in Structural Biology, 1992
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifsNature, 1990
- Escherichia coli phenylalanyl-tRNA synthetase operon is controlled by attenuation in vivoJournal of Molecular Biology, 1983
- Biotin: Biogenesis, Transport, and Their RegulationPublished by Wiley ,1973