Refined structure of elongation factor EF-Tu from Escherichia coli.
The crystal structure of trypsin-modified elongation factor Tu from Escherichia coli, in complex with the cofactor guanosine diphosphate has been refined to a crystallographic R-factor of 19.3%, at 2.6 A resolution. In the model described, the root-mean-square deviation from ideality is 0.019 A for bond distances and 3.9 degrees for angles. The protein consists of three domains: an alpha/beta domain (residues 1 to 200), containing the binding site of the GDP cofactor, and consisting of a six-stranded beta-pleated sheet, six alpha-helices, and two all-beta domains (residues 209 to 299 and 300 to 393), belonging to the tertiary structural class of antiparallel beta-barrels. The GDP-binding domain has a folding that is found in other GDP-binding proteins. Elongation factor Tu interacts with proteins, nucleic acids and nucleotides, making this molecule well suited as a model system for the study of these interactions.
Kjeldgaard
M
M
Department of Chemistry, Aarhus University, Denmark.
Nyborg
J
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000737:chemistry*; D019204:GTP-Binding Proteins / Q000737:chemistry; D006147:Guanine / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006860:Hydrogen Bonding; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D011487:Protein Conformation; D016283:Proto-Oncogene Proteins p21(ras) / Q000378:metabolism; D012266:Ribose / Q000378:metabolism; D016415:Sequence Alignment; D014961:X-Ray Diffraction
D010710:Phosphates; D006153:Guanosine Diphosphate; D006147:Guanine; D012266:Ribose; D019204:GTP-Binding Proteins; D010444:Peptide Elongation Factor Tu; D016283:Proto-Oncogene Proteins p21(ras); D008274:Magnesium