Effect of trypsin modification of the Escherichia coli elongation factor Tu on the ternary complex with aminoacyl-tRNA.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)39406-1 ◽

1985 ◽

Vol 260 (15) ◽

pp. 8702-8705 ◽

Author(s):

E Masuda ◽

A Louie ◽

F Jurnak

Keyword(s):

Escherichia Coli ◽

Ternary Complex ◽

Elongation Factor ◽

Elongation Factor Tu

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The role of Glu259 in Escherichia coli elongation factor Tu in ternary complex formation

Protein Engineering Design and Selection ◽

10.1093/protein/11.2.101 ◽

1998 ◽

Vol 11 (2) ◽

pp. 101-108 ◽

Author(s):

G. N. Pedersen ◽

T. Rattenborg ◽

C. R. Knudsen ◽

B. F. Clark

Keyword(s):

Escherichia Coli ◽

Complex Formation ◽

Ternary Complex ◽

Elongation Factor ◽

Elongation Factor Tu ◽

Ternary Complex Formation

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The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)43845-2 ◽

1983 ◽

Vol 258 (23) ◽

pp. 14200-14205 ◽

Author(s):

A Pingoud ◽

F U Gast ◽

W Block ◽

F Peters

Keyword(s):

Escherichia Coli ◽

Ternary Complex ◽

Elongation Factor ◽

Elongation Factor Tu ◽

Guanosine Tetraphosphate

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The elongation factor Tu coded by the tufA gene of Escherichia coli K-12 is almost identical to that coded by the tufB gene.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)71878-4 ◽

1977 ◽

Vol 252 (6) ◽

pp. 2154-2157 ◽

Author(s):

A V Furano

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu ◽

K 12 ◽

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Stimulation of Escherichia coli adenylate cyclase activity by elongation factor Tu, a GTP-binding protein essential for protein synthesis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)67263-1 ◽

1986 ◽

Vol 261 (25) ◽

pp. 11448-11451

Author(s):

P Reddy ◽

D Miller ◽

A Peterkofsky

Keyword(s):

Escherichia Coli ◽

Protein Synthesis ◽

Adenylate Cyclase ◽

Elongation Factor ◽

Cyclase Activity ◽

Adenylate Cyclase Activity ◽

Elongation Factor Tu ◽

Gtp Binding Protein ◽

Gtp Binding ◽

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Biochemical and structural studies of the tetragonal crystalline modification of the Escherichia coli elongation factor Tu.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)43636-8 ◽

1980 ◽

Vol 255 (14) ◽

pp. 6751-6757

Author(s):

F. Jurnak ◽

A. McPherson ◽

A.H. Wang ◽

A. Rich

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu ◽

Structural Studies ◽

Crystalline Modification

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Bulk preparation and crystallization of the Escherichia coli elongation factor Tu-Ts complex

Analytical Biochemistry ◽

10.1016/0003-2697(85)90466-x ◽

1985 ◽

Vol 150 (1) ◽

pp. 243-248 ◽

Author(s):

Marilyn Yoder ◽

Clare Tores ◽

Robin Corelli ◽

Frances Jurnak

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu

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Uncoupler-induced relocation of elongation factor Tu to the outer membrane in an uncoupler-resistant mutant of Escherichia coli

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/0005-2736(86)90009-x ◽

1986 ◽

Vol 856 (1) ◽

pp. 50-58 ◽

Author(s):

Edward G. Sedgwick ◽

Philip D. Bragg

Keyword(s):

Escherichia Coli ◽

Outer Membrane ◽

Elongation Factor ◽

Resistant Mutant ◽

Elongation Factor Tu

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The Complex Formation between Escherichia coli Aminoacyl-tRNA, Elongation Factor Tu and GTP. The Effect of the Side-Chain of the Amino Acid Linked to tRNA

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1980.tb04714.x ◽

1980 ◽

Vol 108 (1) ◽

pp. 213-221 ◽

Author(s):

Thomas WAGNER ◽

Mathias SPRINZL

Keyword(s):

Escherichia Coli ◽

Complex Formation ◽

Elongation Factor ◽

Elongation Factor Tu

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Dynamics and morphology of the in vitro polymeric form of elongation factor Tu from Escherichia coli

Biochimica et Biophysica Acta (BBA) - General Subjects ◽

10.1016/0304-4165(96)00054-2 ◽

1996 ◽

Vol 1291 (2) ◽

pp. 122-130 ◽

Author(s):

Michael K. Helms ◽

Gerard Marriott ◽

William H. Sawyer ◽

David M. Jameson

Keyword(s):

Escherichia Coli ◽

Elongation Factor ◽

Elongation Factor Tu ◽

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Small-angle neutron scattering study of the ternary complex formed between bacterial elongation factor Tu, guanosine 5'-triphosphate, and valyl-tRNAVal

Biochemistry ◽

10.1021/bi00360a027 ◽

1986 ◽

Vol 25 (12) ◽

pp. 3655-3659 ◽

Author(s):

Bruno Antonsson ◽

Reuben Leberman ◽

Bernard Jacrot ◽

Giuseppe Zaccai

Keyword(s):

Neutron Scattering ◽

Small Angle ◽

Small Angle Neutron Scattering ◽

Ternary Complex ◽

Elongation Factor ◽

Elongation Factor Tu ◽

Scattering Study ◽

Neutron Scattering Study

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