Three-dimensional models of the GDP and GTP forms of the guanine nucleotide domain of Escherichia coli elongation factor Tu.
Three-dimensional models of the GDP and GTP forms of the guanine nucleotide domain of Escherichia coli elongation factor Tu have been derived from the atomic coordinates of the trypsin-modified form of EF-Tu-GDP and by comparison with the ras p21 structures. The significance of the differences in the guanine nucleotide binding sites of EF-Tu and ras p21 are discussed. Crystallization of the EF-Tu-GMPPNP complex is reported.
Jurnak
F
F
Department of Biochemistry, University of California, Riverside 92521.
Heffron
S
S
Schick
B
B
Delaria
K
K
D000595:Amino Acid Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000737:chemistry; D006153:Guanosine Diphosphate / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006165:Guanylyl Imidodiphosphate / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D016283:Proto-Oncogene Proteins p21(ras) / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid; D013912:Threonine; D014357:Trypsin
D010446:Peptide Fragments; D006153:Guanosine Diphosphate; D013912:Threonine; D006165:Guanylyl Imidodiphosphate; D006160:Guanosine Triphosphate; D014357:Trypsin; D019204:GTP-Binding Proteins; D010444:Peptide Elongation Factor Tu; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)