1s72: Difference between revisions

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New page: left|200px<br /><applet load="1s72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s72, resolution 2.40Å" /> '''REFINED CRYSTAL STRU...
 
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[[Image:1s72.gif|left|200px]]<br /><applet load="1s72" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1s72.gif|left|200px]]<br /><applet load="1s72" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1s72, resolution 2.40&Aring;" />
caption="1s72, resolution 2.40&Aring;" />
'''REFINED CRYSTAL STRUCTURE OF THE HALOARCULA MARISMORTUI LARGE RIBOSOMAL SUBUNIT AT 2.4 ANGSTROM RESOLUTION'''<br />
'''REFINED CRYSTAL STRUCTURE OF THE HALOARCULA MARISMORTUI LARGE RIBOSOMAL SUBUNIT AT 2.4 ANGSTROM RESOLUTION'''<br />


==Overview==
==Overview==
The structures of ribosomal proteins and their interactions with RNA have, been examined in the refined crystal structure of the Haloarcula, marismortui large ribosomal subunit. The protein structures fall into six, groups based on their topology. The 50S subunit proteins function, primarily to stabilize inter-domain interactions that are necessary to, maintain the subunit's structural integrity. An extraordinary variety of, protein-RNA interactions is observed. Electrostatic interactions between, numerous arginine and lysine residues, particularly those in tail, extensions, and the phosphate groups of the RNA backbone mediate many, protein-RNA contacts. Base recognition occurs via both the minor groove, and widened major groove of RNA helices, as well as through hydrophobic, binding pockets that capture bulged nucleotides and through insertion of, amino acid residues into hydrophobic crevices in the RNA. Primary binding, sites on contiguous RNA are identified for 20 of the 50S ribosomal, proteins, which along with few large protein-protein interfaces, suggest, the order of assembly for some proteins and that the protein extensions, fold cooperatively with RNA. The structure supports the hypothesis of, co-transcriptional assembly, centered around L24 in domain I. Finally, comparing the structures and locations of the 50S ribosomal proteins from, H.marismortui and D.radiodurans revealed striking examples of molecular, mimicry. These comparisons illustrate that identical RNA structures can be, stabilized by unrelated proteins.
The structures of ribosomal proteins and their interactions with RNA have been examined in the refined crystal structure of the Haloarcula marismortui large ribosomal subunit. The protein structures fall into six groups based on their topology. The 50S subunit proteins function primarily to stabilize inter-domain interactions that are necessary to maintain the subunit's structural integrity. An extraordinary variety of protein-RNA interactions is observed. Electrostatic interactions between numerous arginine and lysine residues, particularly those in tail extensions, and the phosphate groups of the RNA backbone mediate many protein-RNA contacts. Base recognition occurs via both the minor groove and widened major groove of RNA helices, as well as through hydrophobic binding pockets that capture bulged nucleotides and through insertion of amino acid residues into hydrophobic crevices in the RNA. Primary binding sites on contiguous RNA are identified for 20 of the 50S ribosomal proteins, which along with few large protein-protein interfaces, suggest the order of assembly for some proteins and that the protein extensions fold cooperatively with RNA. The structure supports the hypothesis of co-transcriptional assembly, centered around L24 in domain I. Finally, comparing the structures and locations of the 50S ribosomal proteins from H.marismortui and D.radiodurans revealed striking examples of molecular mimicry. These comparisons illustrate that identical RNA structures can be stabilized by unrelated proteins.


==About this Structure==
==About this Structure==
1S72 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with MG, K, NA, CD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S72 OCA].  
1S72 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S72 OCA].  


==Reference==
==Reference==
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[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Klein, D.J.]]
[[Category: Klein, D J.]]
[[Category: Moore, P.B.]]
[[Category: Moore, P B.]]
[[Category: Schmeing, T.M.]]
[[Category: Schmeing, T M.]]
[[Category: Steitz, T.A.]]
[[Category: Steitz, T A.]]
[[Category: CD]]
[[Category: CD]]
[[Category: CL]]
[[Category: CL]]
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[[Category: rna-rna]]
[[Category: rna-rna]]


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