𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Structural comparison of the prokaryotic ribosomal proteins L7/L12 and L30

✍ Scribed by Dr. Marie Leijonmarck; Krzysztof Appelt; John Badger; Anders Liljas; Keith S. Wilson; Stephen W. White

Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
791 KB
Volume
3
Category
Article
ISSN
0887-3585

No coin nor oath required. For personal study only.

✦ Synopsis

The structures of two prokaryotic ribosomal proteins, the carboxyterminal half of L7/L12 from Escherichia coli (L12CTF) and L30 from Bacilus stearothermophilus display a remarkably similar fold in which alpha-helices pack onto one side of an antiparallel, three-stranded, beta-pleated sheet. A detailed comparison of the structures by least-squares methods reveals that more than two-thirds of the alpha carbons can be superimposed with a root mean square distance of 2.33 A. The principal difference is an extra alpha-helix in L12CTF. The sequences of the proteins display a distinct conservation in regions which are crucial to the common fold, in particular the hydrophobic core. It is proposed that the similarity is a result of divergent evolution.

πŸ“œ SIMILAR VOLUMES

The quantitation of ribosome-bound Esche
The quantitation of ribosome-bound Escherichia coli ribosomal protein L7L12 by radial immunodiffusion
✍ Jeremiah J. Morrissey; Paul Caldwell; Herbert Weissbach; Nathan Brot πŸ“‚ Article πŸ“… 1976 πŸ› Elsevier Science 🌐 English βš– 577 KB

A method is described by which ribosomal proteins L7L12 may be immunologically quantitated in the range of lo-75 pmol of protein. With this procedure the amount of ribosomal protein may be conveniently determined on the ribosome or in the postribosomal supernatant.