Methionyl-tRNA synthetase from E. coli--a review.
Methionyl-tRNA synthetase (MetRS) from E coli is a dimer composed of 2 identical subunits of Mr 76 kDa. A fully active monomeric fragment (64 kDa) could be obtained by mild proteolysis of the native dimer. Earlier studies reviewed in Blanquet et al (1979) have compared the catalytic mechanisms of native and trypsin-modified MetRS. Moreover, the truncated form of the enzyme was crystallized and its 3-D structure solved at low resolution. In the last few years, the availability of the corresponding metG gene has facilitated the development of studies using affinity labelling and site-directed mutagenesis techniques. In parallel, the 3-D structure has been solved at a resolution of 2.5 A. These convergent approaches have allowed significant progress in the understanding of the structure-function relationships of this enzyme, and, in particular, of the rules governing the recognition of tRNA.
Meinnel
T
T
Laboratoire de Biochimie URA CNRS 240, Palaiseau, France.
Mechulam
Y
Y
Dardel
F
F
Schmitter
J M
JM
Hountondji
C
C
Brunie
S
S
Dessen
P
P
Fayat
G
G
Blanquet
S
S
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008715:Methionine / Q000494:pharmacology; D008718:Methionine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012343:RNA, Transfer / Q000378:metabolism; D014961:X-Ray Diffraction
D012343:RNA, Transfer; D008715:Methionine; D008718:Methionine-tRNA Ligase