 |
|
Title
|
|
Crystal structure of the ribosome recycling factor from Escherichia coli.
|
|
|
Authors
|
|
K.K.Kim,
K.Min,
S.W.Suh.
|
|
|
Ref.
|
|
EMBO J, 2000,
19,
2362-2370.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|