The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.
The crystal structure of the large ribosomal subunit from Haloarcula marismortui is determined at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins.
The structural basis of ribosome activity in peptide bond synthesis.
It is established that the ribosome is a ribozyme and the catalytic properties of its all-RNA active site are addressed and the mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases.
Somatic mutations in ATP1A1 and CACNA1D underlie a common subtype of adrenal hypertension
Exome sequencing of zona glomerulosa–like APAs identifies nine with somatic mutations in either ATP1A1, encoding the Na+/K+ ATPase α1 subunit, or CACNA1D, encoding Cav1.3, which caused inward leak currents under physiological conditions and induced a shift of voltage-dependent gating to more negative voltages, suppressed inactivation or increased currents.
Crystal structure of the sodium–potassium pump
The X-ray crystal structure of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the α-subunit is presented.
Crystal Structure of the Ternary Complex of Phe-tRNAPhe, EF-Tu, and a GTP Analog
The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving “molecular mimicry” in the translational apparatus.
The structures of four macrolide antibiotics bound to the large ribosomal subunit.
Crystal structure of a copper-transporting PIB-type ATPase
The structure of a PIB-ATPase, a Legionella pneumophila CopA Cu+-ATpase, in a copper-free form, is presented, as determined by X-ray crystallography at 3.2 Å resolution, and indicates a three-stage copper transport pathway involving several conserved residues.
The structural basis of calcium transport by the calcium pump
Functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase are presented, representing the phosphoenzyme intermediates associated withCa2+ binding, Ca2- translocation and dephosphorylation, that are based on complexes with a functional ATP analogue, beryllium fluoride and aluminium fluoride, respectively.
Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM
- J. Sengupta, J. Nilsson, R. Gursky, C. Spahn, P. Nissen, J. Frank
- BiologyNature Structural &Molecular Biology
- 1 October 2004
The results of a cryo-EM study of the 80S ribosome are presented that positively locate RACK1 on the head region of the 40S subunit, in the immediate vicinity of the mRNA exit channel.
Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
A cryo-electron microscopy study presents a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome, and proposes a mechanism to facilitate codon recognition by the incoming aa-tRNA and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu.