1is1: Difference between revisions
New page: left|200px<br /><applet load="1is1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1is1, resolution 2.20Å" /> '''Crystal structure of... |
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[[Image:1is1.gif|left|200px]]<br /><applet load="1is1" size=" | [[Image:1is1.gif|left|200px]]<br /><applet load="1is1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1is1, resolution 2.20Å" /> | caption="1is1, resolution 2.20Å" /> | ||
'''Crystal structure of ribosome recycling factor from Vibrio parahaemolyticus'''<br /> | '''Crystal structure of ribosome recycling factor from Vibrio parahaemolyticus'''<br /> | ||
==Overview== | ==Overview== | ||
X-ray and NMR analyses on ribosome recycling factors (RRFs) from | X-ray and NMR analyses on ribosome recycling factors (RRFs) from thermophilic bacteria showed that they display a tRNA-like L-shaped conformation consisting of two domains. Since then, it has been accepted that domain I, consisting of a three-helix bundle, corresponds to the anticodon arm of tRNA and domain II and a beta/alpha/beta sandwich structure, corresponds to the acceptor arm. In this study, we obtained a RRF from a mesophilic bacterium, Vibrio parahaemolyticus, by gene cloning and carried out an x-ray analysis on it at 2.2 A resolution. This RRF was shown to be active in an in vitro assay system using Escherichia coli polysomes and elongation factor G (EF-G). In contrast, the above-mentioned RRFs from thermophilic bacteria were inactive in such a system. Analysis of the relative orientations between the two domains in the structures of various RRFs, including this RRF from mesophilic bacterium, revealed that domain II rotates about the long axis of the helix bundle of domain I. To elucidate the ribosome binding site of RRF, the peptide fragment (RRF-DI) corresponding to domain I of RRF was expressed and characterized. RRF-DI is bound to 70 S ribosome and the 50 S subunit with an affinity similar to that of wild-type RRF. But it does not bind to the 30 S subunit. These findings caused us to reinvestigate the concept of the mimicry of RRF to tRNA and to propose a new model where domain I corresponds to the acceptor arm of tRNA and domain II corresponds to the anticodon arm. This is just the reverse of a model that is now widely accepted. However, the new model is in better agreement with published biological findings. | ||
==About this Structure== | ==About this Structure== | ||
1IS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http:// | 1IS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: translation]] | [[Category: translation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:59 2008'' | ||
Revision as of 14:15, 21 February 2008
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Crystal structure of ribosome recycling factor from Vibrio parahaemolyticus
OverviewOverview
X-ray and NMR analyses on ribosome recycling factors (RRFs) from thermophilic bacteria showed that they display a tRNA-like L-shaped conformation consisting of two domains. Since then, it has been accepted that domain I, consisting of a three-helix bundle, corresponds to the anticodon arm of tRNA and domain II and a beta/alpha/beta sandwich structure, corresponds to the acceptor arm. In this study, we obtained a RRF from a mesophilic bacterium, Vibrio parahaemolyticus, by gene cloning and carried out an x-ray analysis on it at 2.2 A resolution. This RRF was shown to be active in an in vitro assay system using Escherichia coli polysomes and elongation factor G (EF-G). In contrast, the above-mentioned RRFs from thermophilic bacteria were inactive in such a system. Analysis of the relative orientations between the two domains in the structures of various RRFs, including this RRF from mesophilic bacterium, revealed that domain II rotates about the long axis of the helix bundle of domain I. To elucidate the ribosome binding site of RRF, the peptide fragment (RRF-DI) corresponding to domain I of RRF was expressed and characterized. RRF-DI is bound to 70 S ribosome and the 50 S subunit with an affinity similar to that of wild-type RRF. But it does not bind to the 30 S subunit. These findings caused us to reinvestigate the concept of the mimicry of RRF to tRNA and to propose a new model where domain I corresponds to the acceptor arm of tRNA and domain II corresponds to the anticodon arm. This is just the reverse of a model that is now widely accepted. However, the new model is in better agreement with published biological findings.
About this StructureAbout this Structure
1IS1 is a Single protein structure of sequence from Vibrio parahaemolyticus. Full crystallographic information is available from OCA.
ReferenceReference
Structure and binding mode of a ribosome recycling factor (RRF) from mesophilic bacterium., Nakano H, Yoshida T, Uchiyama S, Kawachi M, Matsuo H, Kato T, Ohshima A, Yamaichi Y, Honda T, Kato H, Yamagata Y, Ohkubo T, Kobayashi Y, J Biol Chem. 2003 Jan 31;278(5):3427-36. Epub 2002 Oct 30. PMID:12411440
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