1EK8

CRYSTAL STRUCTURE OF THE RIBOSOME RECYCLING FACTOR (RRF) FROM ESCHERICHIA COLI

Summary for 1EK8

• Entry DOI: 10.2210/pdb1ek8/pdb
• Descriptor: RIBOSOME RECYCLING FACTOR, MERCURY (II) ION, DECYLOXY-METHANOL, ... (4 entities in total)
• Functional Keywords: ribosome, translation factor, t-rna mimicry, coiled coil, translation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 21461.70

Authors

Min, K.,Suh, S.W.,Kim, K.K. (deposition date: 2000-03-07, release date: 2001-03-07, Last modification date: 2024-02-07)

Primary citation

Kim, K.K.,Min, K.,Suh, S.W.
Crystal structure of the ribosome recycling factor from Escherichia coli.
EMBO J., 19:2362-2370, 2000

PubMed Abstract: We have determined the crystal structure of the Escherichia coli ribosome recycling factor (RRF), which catalyzes the disassembly of the termination complex in protein synthesis. The L-shaped molecule consists of two domains: a triple-stranded antiparallel coiled-coil and an alpha/beta domain. The coil domain has a cylindrical shape and negatively charged surface, which are reminiscent of the anticodon arm of tRNA and domain IV of elongation factor EF-G. We suggest that RRF binds to the ribosomal A-site through its coil domain, which is a tRNA mimic. The relative position of the two domains is changed about an axis along the hydrophobic cleft in the hinge where the alkyl chain of a detergent molecule is bound. The tRNA mimicry and the domain movement observed in RRF provide a structural basis for understanding the role of RRF in protein synthesis.

PubMed: 10811627
DOI: 10.1093/emboj/19.10.2362

Experimental method

X-RAY DIFFRACTION (2.3 Å)