A detailed view of a ribosomal active site: the structure of the L11-RNA complex
Article Abstract:
A study was conducted to examine the crystal structure of the ribosomal protein L11 obtained from the hypethermophilic eubacterium Thermotoga maritima. Results revealed that RNA is tightly bounded to the C-terminal domain of L11 while its N-terminal domain only has limited RNA contacts. It was also observed that mutations conferring resistance to the antibiotics, thiostrepton and micrococcin, occur in the narrow cleft between the RNA and the N-terminal domain.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ
Article Abstract:
X-ray crystallographic structures of the complexed and peptide-free third PDZ domain from the synaptic protein PDS-95 indicate that a four-residue C-terminal region links the PDZ domain with a beta sheet of the domain. A Gly-Leu-Gly-Phe loop plays a major role in binding the C-terminal carboxylate group of the peptide. The mechanisms and molecular basis of recognition and binding of the PDZ domain to the C-terminus of membrane proteins is discussed.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
Article Abstract:
Results describe the three-dimensional X-ray crystallographic structures of the small 30S ribosomal subunit of Thermus thermophilus complexed with antibiotics tetracycline, pactamycin, and hygromycin B. Data indicate that the antibiotics bind to different regions of the ribosome subunit and often exhibiting dissimilarities with those of previously determined antibiotic complexes.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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