2om7: Difference between revisions

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==Overview==

Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome., Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A, resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at, 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from, previous EF-G structures, and in the context of the cryo-EM structure, the, conformational changes are associated with ribosome binding and activation, of the GTP binding pocket. The P loop and switch II approach A2660-A2662, in helix 95 of the 23S rRNA, indicating an important role for these, conserved bases. Furthermore, the ordering of the functionally important, switch I and II regions, which interact with the bound GTP, is dependent, on interactions with the ribosome in the ratcheted conformation., Therefore, a network of interaction with the ribosome establishes the, active GTP conformation of EF-G and thus facilitates GTP hydrolysis and, tRNA translocation.

Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.

==About this Structure==

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[[Category: Protein complex]]

[[Category: Thermus thermophilus]]

[[Category: Connell, S.R.]]

[[Category: Connell, S R.]]

[[Category: Dabrowski, M.]]

[[Category: Fucini, P.]]

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[[Category: Rost, M.]]

[[Category: Schueler, M.]]

[[Category: Spahn, C.M.T.]]

[[Category: Spahn, C M.T.]]

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

[[Category: Wilson, D N.]]

[[Category: ribosome]]

[[Category: rna-protein complex]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:12 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome., Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A, resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at, 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from, previous EF-G structures, and in the context of the cryo-EM structure, the, conformational changes are associated with ribosome binding and activation, of the GTP binding pocket. The P loop and switch II approach A2660-A2662, in helix 95 of the 23S rRNA, indicating an important role for these, conserved bases. Furthermore, the ordering of the functionally important, switch I and II regions, which interact with the bound GTP, is dependent, on interactions with the ribosome in the ratcheted conformation., Therefore, a network of interaction with the ribosome establishes the, active GTP conformation of EF-G and thus facilitates GTP hydrolysis and, tRNA translocation.
+Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Thermus thermophilus]]
-[[Category: Connell, S.R.]]
+[[Category: Connell, S R.]]
 [[Category: Dabrowski, M.]]
 [[Category: Fucini, P.]]
@@ Line 20: / Line 20: @@
 [[Category: Rost, M.]]
 [[Category: Schueler, M.]]
-[[Category: Spahn, C.M.T.]]
+[[Category: Spahn, C M.T.]]
-[[Category: Wilson, D.N.]]
+[[Category: Wilson, D N.]]
 [[Category: ribosome]]
 [[Category: rna-protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:06:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:12 2008''