Heterodimeric GTPase Core of the SRP Targeting Complex

Two structurally homologous guanosine triphosphatase (GTPase) domains interact directly during signal recognition particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The 2.05 angstrom structure of a complex of the NG GTPase domains of Ffh and FtsY reveals a remarkably symm...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2004-01, Vol.303 (5656), p.373-377
Hauptverfasser:	Focia, Pamela J., Shepotinovskaya, Irina V., Seidler, James A., Freymann, Douglas M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Active sites Activity Units Amino Acid Motifs Amino acids Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biochemistry Biological and medical sciences Catalysis Crystalline structure Crystallography, X-Ray Dimerization Drug interactions Ffh protein FtsY protein Fundamental and applied biological sciences. Psychology Guanosine Triphosphate - analogs & derivatives Guanosine Triphosphate - metabolism Heterotrimeric GTP-Binding Proteins - chemistry Heterotrimeric GTP-Binding Proteins - metabolism Hydrogen Hydrogen Bonding Hydrogen bonds Hydrolysis Hydrophobic and Hydrophilic Interactions Latches Literary Devices Membranes Models, Molecular Molecular biology Molecular biophysics Molecules Monomers Nucleotides Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Protein Subunits Proteins Receptors, Cytoplasmic and Nuclear - chemistry Receptors, Cytoplasmic and Nuclear - metabolism Scientific Concepts Signal Recognition Particle - chemistry Signal Recognition Particle - metabolism Structure in molecular biology Thermus - chemistry
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