Structural determination of the functional sites of E. coli elongation factor Tu.
Recently, we have made significant progress in solving the structure of a nicked form of elongation factor (EF)-Tu complexed with GDP. The structure has been refined to an R factor of 19.2% at 2.6 A resolution, so that most of the structure is clearly visible in the electron density map. Here we describe what is known about functional sites of EF-Tu in terms of the structure, which still lacks amino acids 40-60.
Department of Chemistry, Aarhus University, Denmark.
B F
BF
Clark
M
M
Kjeldgaard
T F
TF
la Cour
S
S
Thirup
J
J
Nyborg
D000900:Anti-Bacterial Agents / Q000378:metabolism; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism; D008958:Models, Molecular; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D011728:Pyridones / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D014961:X-Ray Diffraction
D000900:Anti-Bacterial Agents; D011728:Pyridones; D012346:RNA, Transfer, Amino Acyl; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu; C008536:mocimycin