1qvf
From Proteopedia
(New page: 200px<br /><applet load="1qvf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qvf, resolution 3.1Å" /> '''Structure of a deacyl...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qvf.jpg|left|200px]]<br /><applet load="1qvf" size=" | + | [[Image:1qvf.jpg|left|200px]]<br /><applet load="1qvf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qvf, resolution 3.1Å" /> | caption="1qvf, resolution 3.1Å" /> | ||
'''Structure of a deacylated tRNA minihelix bound to the E site of the large ribosomal subunit of Haloarcula marismortui'''<br /> | '''Structure of a deacylated tRNA minihelix bound to the E site of the large ribosomal subunit of Haloarcula marismortui'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During translation, tRNAs cycle through three binding sites on the | + | During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the Haloarcula marismortui large ribosomal subunit and two different E site substrates: a deacylated tRNA acceptor stem minihelix and a CCA-acceptor end. Both of these tRNA mimics contain analogs of adenosine 76, the component responsible for a large proportion of E site binding affinity. They bind in the center of the loop-extension of protein L44e, and make specific contacts with both L44e and 23S rRNA including bases that are conserved in all three kingdoms of life. These contacts are consistent with the footprinting, protection, and cross-linking data that have identified the E site biochemically. These structures explain the specificity of the E site for deacylated tRNAs, as it is too small to accommodate any relevant aminoacyl-tRNA. The orientation of the minihelix suggests that it may mimic the P/E hybrid state. It appears that the E site on the 50S subunit was formed by only RNA in the last common ancestor of the three kingdoms, since the proteins at the E sites of H. marismortui and Deinucoccus radiodurans large subunits are not homologous. |
==About this Structure== | ==About this Structure== | ||
| - | 1QVF 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:// | + | 1QVF 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=1QVF OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Haloarcula marismortui]] | [[Category: Haloarcula marismortui]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Moore, P | + | [[Category: Moore, P B.]] |
| - | [[Category: Schmeing, T | + | [[Category: Schmeing, T M.]] |
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: CL]] | [[Category: CL]] | ||
| Line 26: | Line 26: | ||
[[Category: rna-rna complex]] | [[Category: rna-rna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:10 2008'' |
Revision as of 12:44, 21 February 2008
|
Structure of a deacylated tRNA minihelix bound to the E site of the large ribosomal subunit of Haloarcula marismortui
Overview
During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the Haloarcula marismortui large ribosomal subunit and two different E site substrates: a deacylated tRNA acceptor stem minihelix and a CCA-acceptor end. Both of these tRNA mimics contain analogs of adenosine 76, the component responsible for a large proportion of E site binding affinity. They bind in the center of the loop-extension of protein L44e, and make specific contacts with both L44e and 23S rRNA including bases that are conserved in all three kingdoms of life. These contacts are consistent with the footprinting, protection, and cross-linking data that have identified the E site biochemically. These structures explain the specificity of the E site for deacylated tRNAs, as it is too small to accommodate any relevant aminoacyl-tRNA. The orientation of the minihelix suggests that it may mimic the P/E hybrid state. It appears that the E site on the 50S subunit was formed by only RNA in the last common ancestor of the three kingdoms, since the proteins at the E sites of H. marismortui and Deinucoccus radiodurans large subunits are not homologous.
About this Structure
1QVF is a Protein complex structure of sequences from Haloarcula marismortui with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit., Schmeing TM, Moore PB, Steitz TA, RNA. 2003 Nov;9(11):1345-52. PMID:14561884
Page seeded by OCA on Thu Feb 21 14:44:10 2008
Categories: Haloarcula marismortui | Protein complex | Moore, P B. | Schmeing, T M. | Steitz, T A. | CD | CL | K | MG | NA | Protein-protein complex | Protein-rna complex | Ribosome 50s | Rna-rna complex
