2d3o: Difference between revisions

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[[Image:2d3o.gif|left|200px]]<br /><applet load="2d3o" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2d3o.gif|left|200px]]<br /><applet load="2d3o" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2d3o, resolution 3.35Å" />

'''Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans'''<br />

==Overview==

This study presents the X-ray structure of the N-terminal binding domain, of the D. radiodurans trigger factor (TF) in complex with the D., radiodurans large ribosomal subunit. At 3.35 A, a complete description of, the interactions with ribosomal proteins L23, L29, and 23S rRNA are, disclosed, many of which differ from those found previously for a, heterologous bacterial-archaeal TF-ribosome complex. The beta hairpin loop, of eubacterial L24, which is shorter in archaeal ribosomes, contacts the, TF and severely diminishes the molecular cradle proposed to exist between, the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic, crevice large enough to accommodate the nascent polypeptide chain., Superimposition of the full-length TF and the signal-recognition particle, (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay, of TF, SRP, and the nascent chain during translation.

This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 A, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of which differ from those found previously for a heterologous bacterial-archaeal TF-ribosome complex. The beta hairpin loop of eubacterial L24, which is shorter in archaeal ribosomes, contacts the TF and severely diminishes the molecular cradle proposed to exist between the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic crevice large enough to accommodate the nascent polypeptide chain. Superimposition of the full-length TF and the signal-recognition particle (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay of TF, SRP, and the nascent chain during translation.

==About this Structure==

2D3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2D3O OCA].

2D3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3O OCA].

==Reference==

Line 16:

[[Category: Buerger, J.]]

[[Category: Fucini, P.]]

[[Category: Hansen, H.A.]]

[[Category: Hansen, H A.]]

[[Category: Harms, J.M.]]

[[Category: Harms, J M.]]

[[Category: McInnes, S.J.]]

[[Category: McInnes, S J.]]

[[Category: Schluenzen, F.]]

[[Category: Tian, P.]]

[[Category: Wilbanks, S.M.]]

[[Category: Wilbanks, S M.]]

[[Category: Wilson, D.N.]]

[[Category: Wilson, D N.]]

[[Category: 50s]]

[[Category: nascent chain]]

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[[Category: trigger factor]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2d3o.gif|left|200px]]<br /><applet load="2d3o" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2d3o.gif|left|200px]]<br /><applet load="2d3o" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2d3o, resolution 3.35&Aring;" />
 '''Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit from D. radiodurans'''<br />
 ==Overview==
-This study presents the X-ray structure of the N-terminal binding domain, of the D. radiodurans trigger factor (TF) in complex with the D., radiodurans large ribosomal subunit. At 3.35 A, a complete description of, the interactions with ribosomal proteins L23, L29, and 23S rRNA are, disclosed, many of which differ from those found previously for a, heterologous bacterial-archaeal TF-ribosome complex. The beta hairpin loop, of eubacterial L24, which is shorter in archaeal ribosomes, contacts the, TF and severely diminishes the molecular cradle proposed to exist between, the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic, crevice large enough to accommodate the nascent polypeptide chain., Superimposition of the full-length TF and the signal-recognition particle, (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay, of TF, SRP, and the nascent chain during translation.
+This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 A, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of which differ from those found previously for a heterologous bacterial-archaeal TF-ribosome complex. The beta hairpin loop of eubacterial L24, which is shorter in archaeal ribosomes, contacts the TF and severely diminishes the molecular cradle proposed to exist between the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic crevice large enough to accommodate the nascent polypeptide chain. Superimposition of the full-length TF and the signal-recognition particle (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay of TF, SRP, and the nascent chain during translation.
 ==About this Structure==
-D3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D3O OCA].
+D3O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3O OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Buerger, J.]]
 [[Category: Fucini, P.]]
-[[Category: Hansen, H.A.]]
+[[Category: Hansen, H A.]]
-[[Category: Harms, J.M.]]
+[[Category: Harms, J M.]]
-[[Category: McInnes, S.J.]]
+[[Category: McInnes, S J.]]
 [[Category: Schluenzen, F.]]
 [[Category: Tian, P.]]
-[[Category: Wilbanks, S.M.]]
+[[Category: Wilbanks, S M.]]
-[[Category: Wilson, D.N.]]
+[[Category: Wilson, D N.]]
 [[Category: 50s]]
 [[Category: nascent chain]]
@@ Line 30: / Line 30: @@
 [[Category: trigger factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:25:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:05 2008''