1w94
From Proteopedia
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| - | [[Image:1w94.gif|left|200px]] | + | [[Image:1w94.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF MIL (MTH680), AN ARCHAEAL IMP4-LIKE PROTEIN''' | + | {{Structure |
| + | |PDB= 1w94 |SIZE=350|CAPTION= <scene name='initialview01'>1w94</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF MIL (MTH680), AN ARCHAEAL IMP4-LIKE PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W94 is a [ | + | 1W94 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15654320 15654320] |
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:53 2008'' |
Revision as of 12:53, 20 March 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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