High resolution crystal structure of bovine mitochondrial EF-tu in complex with GDP

• Published in: Journal of molecular biology Vol. 297; no. 2; pp. 421 - 436
• Main Authors: Andersen, Gregers R, Thirup, Søren, Spremulli, Linda L, Nyborg, Jens
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 24-03-2000
• Subjects: Amino Acid Sequence; Animals; binding; binding proteins; Binding Sites; Cattle; Conserved Sequence; Crystallography, X-Ray; crystals; elongation factor tu; elongation factors; Escherichia coli - chemistry; guanosine diphosphate; Guanosine Diphosphate - metabolism; Hydrogen Bonding; mitochondria; Mitochondria - chemistry; mitochondrial proteins; Models, Molecular; molecular conformation; Molecular Sequence Data; pdb/1d2e; Peptide Elongation Factor Tu - chemistry; Peptide Elongation Factor Tu - metabolism; protein biosynthesis; protein structure; Protein Structure, Secondary; Protein Structure, Tertiary; Rotation; Sequence Alignment; Substrate Specificity; Thermodynamics; Thermus - chemistry; translation; Water - metabolism; X-ray crystallography; X-ray diffraction; EF-Tu; EF-Tu t; mitochondrial proteins; elongation factors; EF-Ts; A-site; aa-tRNA; X-ray crystallography; protein structure; EF-Tu e; protein biosynthesis; EF-Tu m; EF-Ts m; NCS
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1006/jmbi.2000.3564

The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1.94 Å. The structure is similar to that of EF-Tu:GDP from
Escherichia coli and
Thermus aquaticus, but the orientation of the GDP-binding domain 1 is changed relative to domains 2 and 3. Sixteen conserved water molecules common to EF-Tu and other G-proteins in the GDP-binding site are described. These water molecules create a network linking separated parts of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu possibly due to an increased mobility in regions close to the GDP-binding site. The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.