Prediction of the secondary structure of proteins from their amino acid sequence.

https://mmbr.asm.org/content/mmbr/51/3/301.full.pdf

Histonelike proteins of bacteria.

E. coli DNA binding protein HU forms nucleosome-like structure with circular double-stranded DNA

Protein synthesis is catalyzed in the peptidyl transferase center of the ribosome. The structure of the 70S ribosome containing tRNAs now gives insight into the active site of a complete ribosome and reveals a direct interaction between the tRNA substrate and ribosomal proteins. Protein synthesis is catalyzed in the peptidyl transferase center (PTC), located in the large (50S) subunit of the ribosome. No high-resolution structure of the intact ribosome has contained a complete active site including both A- and P-site tRNAs. In addition, although past structures of the 50S subunit have found no ordered proteins at the PTC, biochemical evidence suggests that specific proteins are capable of interacting with the 3′ ends of tRNA ligands. Here we present structures, at 3.6-A and 3.5-A resolution respectively, of the 70S ribosome in complex with A- and P-site tRNAs that mimic pre- and post-peptidyl-transfer states. These structures demonstrate that the PTC is very similar between the 50S subunit and the intact ribosome. They also reveal interactions between the ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.

Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome

The 3-A structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.

3-Å resolution structure of a protein with histone-like properties in prokaryotes

Primary structures of two homologous ribosome-associated DNA-binding proteins of Escherichia coli

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2875%2980349-8

The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2878%2980425-6

Liane Mende

Papers

Primary structures of two homologous ribosome-associated DNA-binding proteins of Escherichia coli

The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes.

The primary structure of protein L13 from the large subunit of Escherichia coli ribosomes.