1w94
From Proteopedia
(New page: 200px<br /><applet load="1w94" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w94, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1w94.gif|left|200px]]<br /><applet load="1w94" size=" | + | [[Image:1w94.gif|left|200px]]<br /><applet load="1w94" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w94, resolution 2.00Å" /> | caption="1w94, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF MIL (MTH680), AN ARCHAEAL IMP4-LIKE PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF MIL (MTH680), AN ARCHAEAL IMP4-LIKE PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA | + | Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their beta-sheet and a central alpha-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1W94 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http:// | + | 1W94 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W94 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Antson, A | + | [[Category: Antson, A A.]] |
| - | [[Category: Ng, C | + | [[Category: Ng, C L.]] |
[[Category: Ortiz-Lombardia, M.]] | [[Category: Ortiz-Lombardia, M.]] | ||
[[Category: brix domain]] | [[Category: brix domain]] | ||
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[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:46 2008'' |
Revision as of 13:41, 21 February 2008
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CRYSTAL STRUCTURE OF MIL (MTH680), AN ARCHAEAL IMP4-LIKE PROTEIN
Overview
Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their beta-sheet and a central alpha-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.
About this Structure
1W94 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of Mil (Mth680): internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases., Ng CL, Waterman D, Koonin EV, Antson AA, Ortiz-Lombardia M, EMBO Rep. 2005 Feb;6(2):140-6. PMID:15654320
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