1ek8

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(New page: 200px<br /><applet load="1ek8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ek8, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1ek8.gif|left|200px]]<br /><applet load="1ek8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ek8.gif|left|200px]]<br /><applet load="1ek8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ek8, resolution 2.3&Aring;" />
caption="1ek8, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF THE RIBOSOME RECYCLING FACTOR (RRF) FROM ESCHERICHIA COLI'''<br />
'''CRYSTAL STRUCTURE OF THE RIBOSOME RECYCLING FACTOR (RRF) FROM ESCHERICHIA COLI'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1EK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HG and DEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EK8 OCA].
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1EK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=DEM:'>DEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EK8 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kim, K.K.]]
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[[Category: Kim, K K.]]
[[Category: Min, K.]]
[[Category: Min, K.]]
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[[Category: Suh, S.W.]]
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[[Category: Suh, S W.]]
[[Category: DEM]]
[[Category: DEM]]
[[Category: HG]]
[[Category: HG]]
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[[Category: translation factor]]
[[Category: translation factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:04:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:36 2008''

Revision as of 10:28, 21 February 2008

Image:1ek8.gif

1ek8, resolution 2.3Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1EK8 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ribosome recycling factor from Escherichia coli., Kim KK, Min K, Suh SW, EMBO J. 2000 May 15;19(10):2362-70. PMID:10811627

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