1DD5

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF

Summary for 1DD5

• Entry DOI: 10.2210/pdb1dd5/pdb
• Descriptor: RIBOSOME RECYCLING FACTOR, ACETIC ACID (3 entities in total)
• Functional Keywords: three-helix bundle, beta-alpha-beta sandwich, ribosome
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm : Q9X1B9
• Total number of polymer chains: 1
• Total formula weight: 21668.13

Authors

Selmer, M.,Al-Karadaghi, S.,Hirokawa, G.,Kaji, A.,Liljas, A. (deposition date: 1999-11-08, release date: 1999-12-22, Last modification date: 2024-02-07)

Primary citation

Selmer, M.,Al-Karadaghi, S.,Hirokawa, G.,Kaji, A.,Liljas, A.
Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic.
Science, 286:2349-2352, 1999

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.

PubMed: 10600747
DOI: 10.1126/science.286.5448.2349

Experimental method

X-RAY DIFFRACTION (2.55 Å)