High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP.
The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1. 94 A. 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.
Andersen
G R
GR
Institute of Molecular and Structural Biology, Aarhus University, Gustav Wiedsvej 10C, Aarhus, DK8000, Denmark.
Thirup
S
S
Spremulli
L L
LL
Nyborg
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry; D006153:Guanosine Diphosphate / Q000378:metabolism*; D006860:Hydrogen Bonding; D008928:Mitochondria / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012399:Rotation; D016415:Sequence Alignment; D013379:Substrate Specificity; D013816:Thermodynamics; D013824:Thermus / Q000737:chemistry; D014867:Water / Q000378:metabolism
D014867:Water; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu