PMID:1542116
| Citation |
Kjeldgaard, M and Nyborg, J (1992) Refined structure of elongation factor EF-Tu from Escherichia coli. J. Mol. Biol. 223:721-42 |
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| Abstract |
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. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Escherichia coli/chemistry; GTP-Binding Proteins/chemistry; Guanine/metabolism; Guanosine Diphosphate/metabolism; Hydrogen Bonding; Magnesium/metabolism; Models, Molecular; Molecular Sequence Data; Mutation; Peptide Elongation Factor Tu/chemistry; Peptide Elongation Factor Tu/genetics; Peptide Elongation Factor Tu/metabolism; Phosphates/metabolism; Protein Conformation; Proto-Oncogene Proteins p21(ras)/metabolism; Ribose/metabolism; Sequence Alignment; X-Ray Diffraction |
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