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Structure of the 30S ribosomal subunit
The crystal structure of the 30S subunit from Thermus thermophilus, refined to 3 Å resolution, is reported, which will facilitate the interpretation in molecular terms of lower resolution structural data on several functional states of the ribosome from electron microscopy and crystallography.
Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit
Crystal structures of the 30S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the antibiotic paromomycin, have been solved
Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
The functional implications of the high-resolution 30S crystal structure are described, and details of the interactions between the 30S subunit and its tRNA and mRNA ligands are inferred, which lead to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process.
Crystal structure of an initiation factor bound to the 30S ribosomal subunit.
The crystal structure of a complex of IF1 and the 30S ribosomal subunit is reported, explaining how localized changes at the ribosome A site lead to global alterations in the conformation of the30S subunit.
The structure of the dynactin complex and its interaction with dynein
The reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin, which is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain.
In vitro reconstitution of a highly processive recombinant human dynein complex
The production of a fully recombinant human dynein complex from a single baculovirus in insect cells and single‐molecule fluorescence microscopy provides insight into a novel mechanism for coordinating cargo binding with long‐distance motor movement.
Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA.
We present a detailed analysis of the protein structures in the 30 S ribosomal subunit from Thermus thermophilus, and their interactions with 16 S RNA based on a crystal structure at 3.05 A
Insights into dynein motor domain function from a 3.3 Å crystal structure
It is shown that the main ATP hydrolysis site in dynein (AAA1) is in a low-nucleotide affinity conformation and nucleotide interactions of the other three sites (AAA2, AAA3 and AAA4) are revealed.