1k8h: Difference between revisions

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New page: left|200px<br /><applet load="1k8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k8h" /> '''NMR Structure of Small Protein B (SmpB) from...
 
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[[Image:1k8h.gif|left|200px]]<br /><applet load="1k8h" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1k8h.gif|left|200px]]<br /><applet load="1k8h" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1k8h" />
caption="1k8h" />
'''NMR Structure of Small Protein B (SmpB) from Aquifex aeolicus'''<br />
'''NMR Structure of Small Protein B (SmpB) from Aquifex aeolicus'''<br />


==Overview==
==Overview==
Small protein B (SmpB) is an essential component of the highly conserved, tmRNA-SmpB system that has the dual function of releasing stalled, ribosomes from damaged messenger RNAs and targeting incompletely, synthesized protein fragments for degradation. Nuclear magnetic resonance, (NMR) analysis of SmpB from Aquifex aeolicus revealed an antiparallel, beta-barrel structure, with three helices packed outside the core of the, barrel. While the overall structure of SmpB appears to be unique, the, structure does contain an embedded oligonucleotide binding fold; in this, respect SmpB has similarity to several other RNA-binding proteins that are, known to be associated with translation, including IF1, ribosomal protein, S17 and the N-terminal domain of aspartyl tRNA synthetase. Conserved amino, acids on the protein surface that are most likely to directly interact, with the tmRNA were identified. The presence of widely separated clusters, of conserved amino acids suggests that SmpB could function either by, stabilizing two distal regions of the tmRNA, or by facilitating an, interaction between the tmRNA and another component of the translational, apparatus.
Small protein B (SmpB) is an essential component of the highly conserved tmRNA-SmpB system that has the dual function of releasing stalled ribosomes from damaged messenger RNAs and targeting incompletely synthesized protein fragments for degradation. Nuclear magnetic resonance (NMR) analysis of SmpB from Aquifex aeolicus revealed an antiparallel beta-barrel structure, with three helices packed outside the core of the barrel. While the overall structure of SmpB appears to be unique, the structure does contain an embedded oligonucleotide binding fold; in this respect SmpB has similarity to several other RNA-binding proteins that are known to be associated with translation, including IF1, ribosomal protein S17 and the N-terminal domain of aspartyl tRNA synthetase. Conserved amino acids on the protein surface that are most likely to directly interact with the tmRNA were identified. The presence of widely separated clusters of conserved amino acids suggests that SmpB could function either by stabilizing two distal regions of the tmRNA, or by facilitating an interaction between the tmRNA and another component of the translational apparatus.


==About this Structure==
==About this Structure==
1K8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K8H OCA].  
1K8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8H OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dong, G.]]
[[Category: Dong, G.]]
[[Category: Hoffman, D.W.]]
[[Category: Hoffman, D W.]]
[[Category: smpb]]
[[Category: smpb]]
[[Category: ssra associated protein]]
[[Category: ssra associated protein]]


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