1lva
From Proteopedia
(New page: 200px<br /><applet load="1lva" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lva, resolution 2.12Å" /> '''Crystal structure of...) |
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| - | [[Image:1lva.gif|left|200px]]<br /><applet load="1lva" size=" | + | [[Image:1lva.gif|left|200px]]<br /><applet load="1lva" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lva, resolution 2.12Å" /> | caption="1lva, resolution 2.12Å" /> | ||
'''Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB'''<br /> | '''Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SelB is an elongation factor needed for the co-translational incorporation | + | SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Structural observations and data in the literature suggest that this change happens upon mRNA binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1LVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with Y1 and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with <scene name='pdbligand=Y1:'>Y1</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Selmer, M.]] | [[Category: Selmer, M.]] | ||
| - | [[Category: Su, X | + | [[Category: Su, X D.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: Y1]] | [[Category: Y1]] | ||
[[Category: winged-helix]] | [[Category: winged-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:46 2008'' |
Revision as of 11:48, 21 February 2008
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Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB
Overview
SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Structural observations and data in the literature suggest that this change happens upon mRNA binding.
About this Structure
1LVA is a Single protein structure of sequence from Moorella thermoacetica with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB., Selmer M, Su XD, EMBO J. 2002 Aug 1;21(15):4145-53. PMID:12145214
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