1DD5 | pdb_00001dd5

Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic.

(1999) Science 286: 2349-2352

• PubMed: 10600747 Search on PubMed
• DOI: https://doi.org/10.1126/science.286.5448.2349
• Primary Citation of Related Structures:  
  1DD5


• PubMed Abstract: 
  

  Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.

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Organizational Affiliation: 
• Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Post Office Box 124, SE-22100 Lund, Sweden.